CURRICULUM VITAE
Department of Chemistry and
Biochemistry
Auburn University
Auburn, AL 36830
TABLE OF CONTENTS
1. Standard
Biographical Data and Summary of Activities
2. Percentage
Breakdown of Duties
3. Honors and
Awards
4. Scholarly
Contributions
A. Teaching
a. Courses Taught
b. Graduate Students Whose Work has been Completed
c. Graduate Students Whose Work is Ongoing
d. Undergraduate Student Research Supervised
B. Research
a. Description
of Research Program
b. Article-Length
Publications
c. Presented
Papers and Lectures
d. Patents
and Inventions
e. Grants
and Contracts
C. Outreach
a. Commentary
b. Activities
and Products
D. Service
a. University
Service
b. Professional
Service
1. A. STANDARD BIOGRAPHICAL DATA |
Ph.D., Biochemistry, Department of Chemistry and Biochemistry,
Utah State University, August 1996, Thesis:
Redox Mediation in
Peroxidase-Catalyzed Oxidation
B.A., Food, Nutrition, and Dietetics; Minor: Chemistry;
University of Northern Colorado, December 1991, Magna Cum Laude
Department Chair, Department of Chemistry and Biochemistry, Auburn
University, Auburn, AL, July 2020 – present.
Professor, Department of Chemistry and Biochemistry, Auburn
University, Auburn, AL, August 2019 – present.
Associate
Professor, Department of Chemistry and
Biochemistry, Auburn University, Auburn, AL, August 2005 – present
Assistant
Professor, Department of Chemistry, Auburn
University, Auburn, AL, September 1999 – July 2005
1. B. SUMMARY OF ACTIVITIES |
|
Teaching (15%) |
|
Courses Taught while at Auburn · SCMH 1010 – Concepts of Science · CHEM 1020 – Survey of Chemistry II · CHEM 1030 – Fundamentals of Chemistry I · BCHE 5180/6180 – General Biochemistry I · BCHE 5190/6190 – General Biochemistry II · BCHE 7200 – Advanced Biochemistry I · BCHE 7220 – Cellular and Molecular Enzymology New Courses Developed
while at Auburn · BCHE 5180/6180 – General Biochemistry I · BCHE 5190/6190 – General Biochemistry II · BCHE 7200 – Advanced Biochemistry I · BCHE 7220 – Cellular and Molecular Enzymology |
Advising (in Career
and while at Auburn) Committees (all at Auburn) · Ph.D. completed: 15 as chair; 47 as member · Ph.D. in progress: 4 as chair; 14 as member · Masters completed: 0 as chair; 7 as member · Undergraduate research advisor: Completed 67;
Current: 1 Teaching/Advising Awards · COSAM Outstanding
Undergraduate Mentor (2020) · Mortar Board Excellence in Teaching (2018) · Dean’s Award for
Outstanding Advisor (2017) · SGA Outstanding Faculty
Member (2015) · Dean’s Award for Outstanding
Teacher (2011) · Golden Key Honor Society
Teaching Award (2001) |
Research (50%) |
|
Research Grants while
at Auburn Extramural Sources · PI: NSF, ACS Petroleum Research Fund · Co-PI: NIH, USDA Intramural Sources · IGP, CRG, PRISM, COSAM Travel, Auburn Biogrant, Small Instrumentation · Start up funds: $160,000 · Other internal funding: $189,120 · Total Extramural funding (PI): $1,064,084 · Total Extramural funding (co-PI): $1,649,165 |
Publications (in
Career and while at Auburn) Peer-Reviewed Research
Publications · Journal Articles: Career, 42; Auburn, 28 · Proceedings/Book Chapters: Career, 4; Auburn 3 · Career Citations: 2608 · H index: 23; i10 index: 34 Presentations (in
Career and while at Auburn) · Invited Talks/Lectures: 36 Career; 31 Auburn · Meeting Presentations: Career, 117; Auburn, 102 Selected Advisee
Awards while at Auburn · Malone-Zallen
Fellowship; Distinguished Dissertation Award; CMB Summer GRA |
Service and outreach (35%) |
|
Service at Auburn DCB · Department Chair · Graduate Program Officer · Departmental Leadership
Council · Graduate Program Committee
Chair · Graduate Program
Assessment Development · Biochemistry Division
Chair COSAM · COSAM Leader selection
committees · CMB Program Graduate
Fellowship Committee University · University Senate
representative for DCB · APA+EP Advisory Council Professional Service · NSF reviewer (ad hoc and
panelist) · Program Chair, 11th
Annual Southeast Enzyme Conference · Treasurer: American
Chemical Society, Auburn Section |
· Reviewer: Proc. Nat. Acad. Sci., J. Am. Chem. Soc., Biochemistry, J. Biol. Chem., J. Inorg. Biochem., PLOS One, Biochim. Biophys. Acta, Biochemie, J. Biol. Inorg.
Chem., Chem. Res. Toxicol. Bioorg.
Med. Chem., et al. Outreach at Auburn Sparks STEM prison lecture
series · Speaker · Faculty
recruiter/organizer · Guide for new faculty
speakers AU Competitive Outreach
Grant · Co-PI prison education
course development Summer Bridge Program
(COSAM) · Undergraduate research
involvement Q and A · Hands-on research demonstration Outreach Awards · COSAM Faculty
Service/Outreach Award (2015) · ACS Outreach Volunteers of
the Year (2014) |
2. PERCENTAGE BREAKDOWN
OF DUTIES |
Teaching, 15% Research, 50% Outreach/Service, 35%
3. HONORS AND AWARDS |
Teaching and Advising Awards
COSAM Outstanding Undergraduate Mentor Award. College of Sciences and Mathematics, 04/20.
Mortar Board Excellence in Teaching Award. Mortar Board National College Senior Honor Society, Sphinx
Chapter, Auburn University, 02/18.
Dean’s Award for Outstanding Advisor. College of Sciences and Mathematics, 04/17.
Student Government Association Outstanding Faculty Member
Award. Auburn University, 04/15.
Final Lecture Nominee. Student Government Association-sponsored student-nominated award. Finalist selected by campus-wide vote of the students. Auburn University, 02/14.
Dean’s Award for Outstanding Teacher. College of Sciences and Mathematics, Auburn University, April 2011.
Alpha Epsilon Delta Honorary National Membership. Awarded by the Auburn University AED Chapter, April 2011.
Golden Key National Honor Society Teaching Award, Golden Key Honor Society, Auburn University Chapter, April 2001.
Outreach Awards
College of Sciences and Mathematics Faculty
Service/Outreach Award. Auburn University,
April 2015.
American Chemical Society Outreach Volunteers of the Year. Auburn Section of the American Chemical Society, February
2014.
Fellowships, Traineeships, and Academic
Awards
Center in Molecular Toxicology Postdoctoral Research Trainee, Department of Biochemistry, Vanderbilt University School of Medicine, 07/98 – 08/99.
Willard L. Eccles Family Foundation Fellow, College of Science, Utah State University, 10/92- 09/95.
E.L. and Inez Waldron Award, Biotechnology Center, Utah State University, 06/96.
George Emert Scholar, Chemistry and Biochemistry, Utah State University, 05/96.
Thomas F. Emery Memorial Research Scholar, Chemistry and Biochemistry, Utah State University, 05/95.
4. SCHOLARLY CONTRIBUTIONS |
4. A. TEACHING |
4.A.a.
Courses Taught
Year |
Semester |
Course |
Title |
Hrs |
Students |
|
2023 |
Fall |
BCHE 5190/6190 |
General Biochemistry II |
3 |
58 |
|
|
Spring |
BCHE 5190/6190 |
General Biochemistry II |
3 |
135 |
|
|
|
|
|
|
|
|
2022 |
Spring |
BCHE 7220 |
Cellular and Molecular Enzymology |
3 |
6 |
|
|
|
|
|
|
|
|
2020 |
Spring |
BCHE 7220 |
Cellular and Molecular Enzymology |
3 |
12 |
|
|
|
|
|
|
|
|
2019 |
Fall |
CHEM 7950 |
Grad Student Orientation Seminar |
1 |
17 |
|
|
Spring |
BCHE 5190/6190 |
General Biochemistry II |
3a |
110 |
|
|
|
|
|
|
|
|
2018 |
Fall |
CHEM 7950 |
Grad Student Orientation Seminar |
1 |
17 |
|
|
Spring |
BCHE 7220 |
Cellular and Molecular Enzymology |
3 |
14 |
|
|
|
|
|
|
|
|
2017 |
Fall |
CHEM 7950 |
Grad Student Orientation Seminar |
1 |
25 |
|
|
Spring |
BCHE 5190/6190 |
General Biochemistry II |
3a |
96 |
|
|
|
|
|
|
|
|
2016 |
Fall |
BCHE 5190/6190 |
General Biochemistry II |
3a |
92 |
|
|
Spring |
BCHE 7220 |
Cellular and Molecular Enzymology |
3 |
10 |
|
aTwo,
two-hour review sessions are offered prior to each exam; Total: 8 sessions or 16
hours/semester
Cumulative Teaching Experience at Auburn:
BCHE 7220 Cellular and Molecular Enzymology (10´, 103 students, ~10 per offering)
BCHE 7200 Advanced Biochemistry I (6´, 145 students, ~24 per offering)
BCHE 5190/6190 General Biochemistry II (14´, 1,318 UG/68 G students, ~96/5 per offering)
BCHE 5180/6180 General Biochemistry I (5´, 639 UG/20 G students, ~128/4 per offering)
BCHE 6190 General Biochemistry II (prior to piggyback split) (6´, 488 students, ~81 per offering
CHEM 1030 Fundamentals of Chemistry I (1´, 211 students)
CHEM 1010 Survey of Chemistry II (1´, 119 students)
SCMH 1010 Concepts of Science (2´, 415 students, ~208 per offering)
CHEM 640 (16 students)/CHEM 646 (18 students) (qtrs, 1´ each – roughly equivalent to BCHE 7200)
The number of Biochemistry Division faculty combined with the number of section offerings for the large BCHE 5180/6180 and BCHE 5190/6190 courses has not enabled division faculty to teach outside of the department’s BCHE courses since 2009.
I was given release time from teaching in Fall 2017 to support progress on a new NSF grant, and to offset the increase in service commitment starting in Summer 2017 as the DBC Graduate Program Officer (GPO). Organizing and executing the New Graduate Student Seminar (Fall semesters) is part of GPO duties. The necessary tasks include soliciting participating faculty (multiple departments/units on campus), scheduling, generating material and presenting for two of the sessions, and monitoring student attendance. Since taking the position of Chair of the Department of Chemistry and Biochemistry, I have retained a diminished role in instruction.
4.A.b.
Graduate students whose work has been completed
4.A.b.1. Dr. Goodwin as major professor
Dr. Tarfi
Aziz, Ph.D. Graduate, Chemistry. December 2022.
Dissertation Title: Investigating a novel
protein-based cofactor: toward elucidating the catalase mechanism of Mycobacterium
tuberculosis KatG. Dr. Aziz is engaged in
postdoctoral research in the laboratory of Dr. Kristine Griffett
in the Department of Anatomy, Physiology, and Pharmacology in the College of
Veterinary Medicine, Auburn University.
Dr. Callie Barton, Ph.D. Graduate, Chemistry. December 2022. Dissertation Title: Catalase-Peroxidase:
A Structure that Facilitates Electron Transfer, Protein-based Cofactor
Formation, and Antibiotic Activation. Anticipating
continuing her career as a lecturer in the Department of Chemistry and
Biochemistry at Auburn University.
Dr.
Md Jahangir Alam, Ph.D.
Graduate, Chemistry, August 2022. Dissertation Title: Evaluation of Bacillus biocontrol potential through the lens of
secondary metabolite diversity in genomic, enzymatic, and chemical space. Continuing career as a postdoctoral
researcher investigating ultrahigh throughput mass spectrometry using rapid
acoustic ejection MS. Dr. Alam is under the direction
of Drs. Paul Harradine and Kevin Bateman.
Dr. Jessica R. Krewall,
Ph.D. Graduate,
Chemistry, September 2021. Dissertation Title: Impact of the oxidizable scaffold of catalase-peroxidase (KatG): Modulation of a heme peroxidase for catalytic
versatility. Continuing career with postdoctoral research at Yale
University under the direction of Dr. Karen Anderson.
Dr.
Hui Xu, Ph.D. Graduate,
Chemistry. Project: August 2020. Dissertation Title: How an
arginine switch promotes the self-preservation of an H2O2-degrading
enzyme KatG: Strategic use of an active site
tryptophan. Dr. Xu continued her career
with postdoctoral research at the University of Texas, San Antonio, under the
direction of Dr. Aimin Liu, and in April 2022, she
moved on to Frontage Laboratories, Inc.
Dr. Rene Ngolui Fuanta, Ph.D. Graduate,
Chemistry, August 2018. Dissertation Title: Transition
from classical methods to new strategies: Mechanistic evaluation of inhibitors
against Mycobacterium tuberculosis shikimate kinase. Continued career and
currently engaged as a tenure-track faculty member in the Department of
Chemistry and Biochemistry at East Stroudsburg University.
Dr. Olive Njuma, Ph.D. Graduate, Chemistry, August 2016.
Dissertation Title: Resolving the
paradoxical nature of a bifunctional enzyme: Pathways and regulation of
intramolecular electron transfer in KatG. Continued
career with postdoctoral research at Vanderbilt University School of Medicine
under the direction of Dr. F. Peter Guengerich.
Currently employed with Molecular Assemblies, Inc., San Diego, CA.
Dr. Haijun Duan, Ph.D. Graduate, Chemistry, December 2014.
Dissertation Title: KatG as a defense against hydrogen peroxide toxicity: from a redundant
C-terminal domain to the paradoxical synergy of two mutually antagonistic
activities. Continued career in postdoctoral research, first at the
University of Kentucky under the direction of Dr. Anne-Frances Miller, and
currently in the Structural Biology Unit of the Van Andel
Institute in Grand Rapids, MI. He is under the direction of the Program Lead,
Dr. Huilin Li.
Dr. Elizabeth Ndontsa, Ph.D. Graduate, Chemistry, May 2013. Dissertation Title: Synergy not antagonism in antioxidant defenses: the unanticipated effect of electron donors on catalase-peroxidase function. (*AU Distinguished Dissertation Award) Continued career as a postdoctoral research associate at Scripps Research Institute and University of California, Berkeley under the direction of Michael Marletta. Currently employed as a Project Manager at Gilead Inc., Berkeley, CA.
Dr. Yu Wang, Ph.D. Graduate, Chemistry, December 2012. Dissertation Title: Gene duplication and fusion: Strategy for active-site control and starting point for new catalysts. Continued career as a postdoctoral researcher at Virginia Tech under the direction of Dr. Robert White. Became a tenure-track faculty member at University of North Georgia and was promoted with tenure to associate professor before electing to pursue an MD at Morehouse Medical School in Atlanta, GA.
Dr. Shalley Kudalkar, Ph.D. Graduate, Chemistry, May 2012. Dissertation Title: Roles of Large Loops in Catalytic Versatility of Catalase-Peroxidases: Significance of Peripheral Structures in Improvising Enzyme Functions. Continued career as a postdoctoral researcher at Vanderbilt University School of Medicine under the direction of Dr. Lawrence J. Marnett. Currently an Associate Research Scientist at the Yale School of Medicine.
Dr. Robert Moore, PhD Graduate, Chemistry, May 2009. Dissertation Title: Toward the Understanding of Complex Biochemical Systems: The Significance of Global Protein Structure and Thorough Parametric Analysis. Continued career as an adjunct faculty member in the Department of Chemistry at Wayland Baptist University. He is currently a tenured full professor in that department.
Dr. Carma Cook, PhD Graduate, Chemistry, May 2009. Dissertation Title: Role of Distant Intrasubunit Residues in Catalase-peroxidase Catalysis: Tracing the role of gene duplication and fusion in enzyme structure and function. Continued career in postdoctoral research at Auburn University, Montgomery. Currently engaged as an Assistant Professor of Chemistry at Chattanooga State Community College.
Dr. Ruletha Baker, Ph.D. Graduate, Chemistry, December 2006. Dissertation Title: Roles of an ‘Inactive’ Domain in Catalase-Peroxidase Catalysis: Modulation of Active Site Architecture and Function by Gene Duplication.
Dr. Cornelius Varnado, Ph.D. Graduate, Chemistry, August 2006. Dissertation Title: Enhancing Expression of Recombinant Hemoproteins: Progress Toward Understanding Structure/Function and Therapeutic Application. Continued career in postdoctoral research at Rice University under the direction of Dr. John Olsen. Currently engaged as a Senior Biologic Process Engineer at Allsource/Merck.
Dr. Yongjiang Li, Ph.D. Graduate, Chemistry, December 2005. Dissertation Title: Roles of Two Interhelical Insertions in Catalase-Peroxidase Catalysis: Tracing the Impact of Peripheral Protein Structures on Heme Enzyme Function. Continued career in postdoctoral research at the National Institutes on Aging at NIH and then as a Research Associate at the Scripps Research Institute. Presently is a Research Scientist in Research and Development at ScienCell Research Laboratories, Inc., San Diego, CA.
Dr. Ronald Marcy, GND Graduate Student, Chemistry, Fall 2002 – Spring 2003. Project: Structure and function of catalase-peroxidases. As an instructor at Alabama Southern Community College, Ron worked weekends in the laboratory to get exposure to the latest techniques in biochemistry and molecular biology in order to enhance teaching of his chemistry and microbiology courses.
4.A.b.2. Dr. Goodwin as advisory
committee member
Student |
Degree/Year |
Discipline |
Advisor |
|
Fnu Ibitsam |
PhD |
2023 |
Drug Discovery Devel |
Dr. A. Kisselev |
Kenny
Nguyen |
PhD |
2023 |
Chemistry |
Dr. Mansoorabadi |
Shadi Yavari |
PhD |
2022 |
Chemistry |
Dr. E. Duin |
Katherine Clohan |
PhD |
2022 |
Chemistry |
Dr. E. Duin |
Bryan Croninb |
- |
2021 |
Chemistry |
Dr. E. Duin |
Jamonica Moore |
PhD |
2022 |
Chemistry |
Dr. C. Goldsmith |
Chioma Helen Alohb |
- |
2021 |
Chemistry |
Dr. H. Ellis |
Shruti Somaib |
- |
2021 |
Chemistry |
Dr. H. Ellis |
Shuxin Li |
PhD |
2021 |
Chemistry |
Dr. Mansoorabadi |
Qi Cui |
PhD |
2021 |
Chemistry |
Dr. J. Harshman |
Trey Slaneyb |
- |
2021 |
Chemistry |
Dr. Mansoorabadi |
Kara Johnson |
PhD |
2020 |
Chemistry |
Dr. B. Merner |
Richard Hagen |
PhD |
2020 |
Chemistry |
Dr. H. Ellis |
Katie Tombrello |
PhD |
2019 |
Chemistry |
Dr. H. Ellis |
Ahmad Almalkia |
PhD |
2019 |
Drug Discovery Devel |
Dr. R. Clark |
Carly Engel |
PhD |
2019 |
Chemistry |
Dr. E. Duin |
Victoria Owens |
PhD |
2019 |
Chemistry |
Dr. Mansoorabadi |
Claire Graham |
PhD |
2018 |
Chemistry |
Dr. H. Ellis |
Kaiyuan Zheng |
PhD |
2018 |
Chemistry |
Dr. Mansoorabadi |
Juan Hu |
PhD |
2018 |
Chemistry |
Dr. C. Easley |
Dianna Forbes |
PhD |
2018 |
Chemistry |
Dr. H. Ellis |
Younis Abiedallaa |
PhD |
2018 |
Drug Discovery Devel |
Dr. R. Clark |
Marike Vissera |
PhD |
2018 |
Veterinary Medicine |
Dr. D. Boothe |
Jonathan Musila |
PhD |
2017 |
Chemistry |
Dr. H. Ellis |
Selamawit Ghebreamlak |
PhD |
2016 |
Chemistry |
Dr. E. Duin |
Lizette Gomez Ramosb |
- |
2015 |
Chem Eng (Ga Tech) |
Dr. A. Bromarius |
Jiansheng Huang |
PhD |
2015 |
Drug Discovery Devel |
Dr. P. Panizzi |
Andrew Damiania |
PhD |
2015 |
Chemical Engineering |
Dr. J. Wang |
Paritosh Dayalb |
- |
2015 |
Chemistry |
Dr. H. Ellis |
Divya Prakash |
PhD |
2014 |
Chemistry |
Dr. E. Duin |
Johayra
Simithya |
PhD |
2014 |
Drug Discovery Devel |
Dr. A. Calderón |
Qiao Zhang |
PhD |
2014 |
Chemistry |
Dr. C. Goldsmith |
Brian Ferguson |
PhD |
2014 |
Kinesiology |
Dr. B. Gladden |
Catherine Njeri |
PhD |
2014 |
Chemistry |
Dr. H. Ellis |
Matthew
Barberio |
PhD |
2013 |
Kinesiology |
Dr. D. Pascoe |
Xiao Xiao |
MS |
2013 |
Chemistry |
Dr. E. Duin |
John “Mick” Robbins |
PhD |
2012 |
Chemistry |
Dr. H. Ellis |
Ann Johnsona |
PhD |
2012 |
Nutrition |
Dr. S. Gropper |
Jingyuan Xiong |
PhD |
2012 |
Chemistry |
Dr. H. Ellis |
Chengdong Huang |
PhD |
2011 |
Chemistry |
Dr. S. Mohanty |
Alejandro Silva |
MS |
2011 |
Animal Sciences |
Dr. F.F. Bartol |
Weiya Xu |
PhD |
2010 |
Chemistry |
Dr. E. Duin |
Jody Burke |
PhD |
2010 |
Animal Sciences |
Dr. J. Wower |
Russell Carpenter |
PhD |
2008 |
Chemistry |
Dr. H. Ellis |
Erin Imsand |
PhD |
2009 |
Chemistry |
Dr. H. Ellis |
Matthew Goodwin |
PhD |
2008 |
Kinesiology |
Dr. B. Gladden |
Mi Wang |
PhD |
2008 |
Chemistry |
Dr. E. Duin |
Weikuan Li |
PhD |
2008 |
Chemistry |
Dr. S. Schneller |
Sidharth Venkatesh |
PhD |
2008 |
Chemical Engineering |
Dr. M. Byrne |
Xuanzhi Zhan |
PhD |
2008 |
Chemistry |
Dr. H. Ellis |
Rajesh Gupta |
PhD |
2008 |
Chemical Engineering |
Dr. Y.Y. Lee |
Na Yang |
PhD |
2007 |
Chemistry |
Dr. E. Duin |
Angelo Karavolosb |
- |
2007 |
Polymer/Fiber Eng |
Dr. Abdel-Hady |
John-Ryan McAnnally |
MS |
2007 |
Biomedical Sciences |
Dr. J. Bradley |
Dolapo Adediji |
PhD |
2007 |
Chemistry |
Dr. E. Duin |
Benlian Gao |
PhD |
2006 |
Chemistry |
Dr. H. Ellis |
Honglei Sun |
MS |
2006 |
Chemistry |
Dr. H. Ellis |
Ling Tang |
PhD |
2006 |
Animal Sciences |
Dr. W. Bergen |
Wei Ye |
PhD |
2005 |
Chemistry |
Dr. S. Schneller |
Chunru Linb |
- |
2005 |
Biological Sciences |
Dr. M. Wooten |
Rong Wu |
PhD |
2005 |
Chemistry |
Dr. S.D. Worley |
Darcy Goodwin |
MS |
2004 |
Animal Sciences |
Dr. F.F. Bartol |
Amanda Bean |
PhD |
2004 |
Chemistry |
Dr. T. Albrecht |
Ben Stronach |
MS |
2001 |
Animal Sciences |
Dr. W. Bergen |
Wendy White |
MS |
2001 |
Biological Sciences |
Dr. M. Wooten |
aDenotes
service as University Reader bStudent
resigned prior to completing degree program |
|
4.A.c.
Graduate students whose work is ongoing
4.A.c.1. Dr.
Goodwin as major professor
Rejaul Islam, Ph.D. Candidate, Chemistry. Development
of mechanistically targeted intrinsic protein fluorescence to elucidate
mechanisms of M. tuberculosis
shikimate kinase inhibition by marine natural products.
Chidozie Ugochukwu, Ph.D. Candidate, Chemistry. Co-directed
with Dr. Holly Ellis of the Department of Biochemistry and Molecular Biology at
the Brody Medical School, East Carolina University. Evaluating the regulatory
and metabolic links between sulfur acquisition and metabolism and defenses
against reactive oxygen species.
Nana Quansah, Ph.D. Student, Chemistry. Engaged in
understanding the biocontrol potential of Bacillus and Paenibacillus
species/strains, including evaluation of antibiosis activity of intact
organisms and extracted metabolites against pathogenic fungi and oomycetes,
evaluation of biosynthetic gene clusters, and characterization of Bacillus
and Paenibacillus-derived compounds with
antimicrobial activity via mass spectrometry and other techniques.
4.A.c.2. Dr. Goodwin as committee member
Student |
Degree (L)a |
Discipline |
Advisor |
Alex
Saunders |
PhD (C) |
Chemistry |
Dr. C. Goldsmith |
Tingting Qu |
PhD (C) |
Chemistry |
Dr. J. Harshman |
Theophila
Dusabamahoro |
PhD (C) |
Chemistry |
Dr. E. Duin |
Kabre Heck |
PhD (C) |
Drug Discovery Devel |
Dr. A Calderón |
Andresa Bezerra |
PhD (C) |
Chemistry |
Dr. C. Easley |
Chidinma Lucy Odili |
PhD (C) |
Chemistry |
Dr. Mansoorabadi |
Prosenjit Ray |
PhD (S) |
Chemistry |
Dr. Mansoorabadi |
Chelsea Rand |
PhD (S) |
Chemistry |
Dr. Mansoorabadi |
Arielle Dallas |
PhD (S) |
Chemistry |
Dr. E. Duin |
Chukwuemeka Okpala |
PhD (S) |
Chemistry |
Dr. E. Duin |
aL –
Level, designates current progress toward degree. C – PhD candidate; S – PhD
student |
|||
|
4.A.d Undergraduate Student Research Supervised (Current in
italics):
Student |
Major |
Dates |
Fellowships |
Reilly Bass |
Biochemistry |
08/23 – present |
|
Braeden Olson |
Biomed Sci |
01/23 – present |
|
Ryan Mumford |
Biochemistry |
08/21 – 5/23 |
Marks |
Nina Orihuela |
BA Chemistry |
08/21 – 5/22 |
Marks |
Benjamin Faulkner |
Chem Eng |
01/21 – 5/22 |
|
Madeleine Forbes |
Chemistry |
08/20 – 11/21 |
|
Raegan Gantt |
BA Chemistry |
01/21 – 04/21 |
|
Monty Greene† |
BA Chemistry |
01/21 – 04/21 |
|
Aishah Lee |
Biochemistry |
05/19 – 08/21 |
NSF, Marks |
Laura
Minton |
Biomed Sci |
03/19 – 05/20 |
Marks |
Melissa
Williams |
Biochemistry |
05/19 – 12/19 |
|
Daniel
Bayer |
BA Chemistry |
03/19 – 07/19 |
|
Savannah
Petrus |
Biochemistry |
01/18 – 05/19 |
Marks |
Patrick Sahrmann |
Biochemistry |
08/16 – 05/19 |
AU URF, Marks |
Kirklin McWhorter |
Biochemistry |
05/17 – 12/18 |
CMB, Haggard |
Michael Skinner |
Biomed Sci |
01/15 – 12/17 |
CMB |
Olivia Snider |
Biochemistry |
05/15 – 05/16 |
CMB |
Theresa Simermeyer |
Biochemistry |
05/15 – 05/16 |
|
Daniel
Zieman |
BA Chemistry |
08/15 – 10/15 |
|
Moneisha
Cunningham |
BA Chemistry |
01/15 – 06/15 |
|
Lauren Barr |
Biomed Sci |
01/14 – 05/15 |
Marks |
Teddy Childers |
Biomed Sci |
01/14 – 12/14 |
|
Ethan McCurdy** |
BA Chemistry |
01/13 – 06/14 |
AU URF |
Gobind Gill* |
Biochemistry |
06/12 – 06/14 |
CMB |
R. Elliot Browning |
Biomed Sci |
01/13 – 12/13 |
|
Jennifer Lewis |
Biomed Sci |
06/12 – 05/13 |
|
Benjamin Jackson |
Biomed Sci |
05/11 – 05/12 |
|
Jordan Suh |
Chemistry |
01/11 – 05/12 |
CMB |
Kristen Henninger |
Chemistry |
09/10 – 05/11 |
|
Kendall Walton |
Chemistry |
09/10 – 05/11 |
|
Sara Ransom* |
Biomed Sci |
05/10 – 05/11 |
CMB |
Thomas Townes |
Biomed Sci |
09/10 – 12/10 |
|
Ryan Tucker |
Biochemistry |
09/09 – 07/10 |
|
John Pribonic |
Biochemistry |
05/09 – 07/09 |
|
Michael Dumas |
Biomed Sci |
05/09 – 09/09 |
|
Corey Prescott |
Chemistry |
01/09 – 05/09 |
|
Robert Campbell |
Biochemistry |
05/08 – 05/09 |
CMB |
JaRyce Nabors |
Biochemistry |
08/07 – 05/08 |
|
Michelle Muldowney |
Biochemistry |
08/07 – 12/08 |
|
Joey Russell |
Biomed Sci |
01/08 – 05/08 |
|
Rachel Williams |
Biochemistry |
01/07 – 12/07 |
|
Jessica Williams |
Biochemistry |
05/07 – 08/07 |
|
Michael Love |
Chemistry |
01/07 – 12/07 |
|
Alex Taylor |
Biochemistry |
08/06 – 12/06 |
|
Luke Powell |
Biochemistry |
08/05 – 12/06 |
COSAM URF |
JaRyce Nabors |
Biochemistry |
05/06 – 08/06 |
EPSCoR |
Jennifer Smith |
Biochemistry |
01/06 – 05/06 |
|
Allan Bagget |
Biomed Sci |
01/06 – 05/06 |
|
Kimberley Laband |
Molecular Biol |
05/03 – 05/05 |
AU URF |
Dan Carter |
Biomed Sci |
09/-04 – 12/04 |
|
Byron Smith |
Biomed Sci |
08/04 – 12/04 |
|
Stephen Pehler |
Molecular Biol |
04/04 – 11/04 |
|
Tyson Kilpatrick |
Biomed Sci |
01/04 – 05/04 |
|
Greyson McGowin |
Biomed Sci |
05/03 – 09/03 |
CMB |
Derek Fortson |
Biochemistry |
09/02 – 05/03 |
COSAM URF |
J. Kenneth Roberts |
Biomed Sci |
06/02 – 05/03 |
|
Sarah Peaslee |
Biochemistry |
06/02 – 05/03 |
|
Melanie Oliver |
Microbiology |
05/02 – 12/02 |
|
Robert Thomas |
Asbury College |
05/02 – 09/02 |
|
Kristin Hertwig |
Biochemistry |
01/00 – 12/02 |
AU URF |
Erika Schansberg |
Microbiology |
09/01 – 05/02 |
|
Thomas Cash |
Chemistry |
01/02 – 05/02 |
|
Matthew McIntyre |
Biomed Sci |
05/01 – 09/01 |
|
Nancy Ruth Wilkins |
Biochemistry |
05/01 – /09/01 |
|
Emily Brantley |
Molecular Biol |
06/00 – 12/01 |
|
Juan Carmona |
Molecular Biol |
09/00 – 05/01 |
|
Amy Wainwright |
Biochemistry |
01/00 – 06/00 |
|
Randy Bootha |
Biochemistry |
05/96 – 09/96 |
|
Joseph Bensona |
Biochemistry |
05/95 – 05/96 |
|
Curtis Takemotoa |
Political Sci |
05/94 – 05/96 |
|
**Dean’s Undergraduate Research Award (2013 – 2014);
NSF GRFP recipient at Columbia University *Honors Thesis completed based on Goodwin laboratory
research †CHEM
2980 requirement filled by DCB Colloquium; DCG
managed assignments and evaluation aResearch completed at Utah State University
|
4.
B. RESEARCH |
4.B.a Description of Research Program
Goodwin laboratory student success. An important measure of the success of this research program is the students who have contributed to its progress over years. Following the completion of their degrees (see 4.A.b.1 Dr. Goodwin as major professor), they have gone on to postdoctoral positions at some of the top institutions and labs in the country, including the National Institutes of Health, the Scripps Research Institute, Vanderbilt, Yale, Berkeley, Rice, University of Kentucky, Virginia Tech, Merck, and others. Several of my former students have since taken tenure-track faculty positions, and others have moved into positions in industry.
Broadly, the central interest of my research is in understanding the connections between enzyme structure and mechanism, including mechanisms of cofactor maturation, catalysis, inhibition, and irreversible inactivation. The enzymes under investigation in my laboratory are intimately connected to important physiological phenomena of substantial biomedical concern. These include host-pathogen interactions, virulence of bacterial and fungal pathogens, antibiotic resistance (particularly in tuberculosis), and the development of new antibiotic agents to fight organisms like Mycobacterium tuberculosis. Consequently, our progress in elucidating the enzyme structure-function connection carries important ramifications for understanding these broader concerns.
Catalase-peroxidase (KatG) Structure and Mechanism. A case-in-point is provided by KatG. The primary function of KatG is to degrade hydrogen peroxide (H2O2). Interestingly, in Mycobacterium tuberculosis (Mtb), KatG is also critical for the activation of the front line antitubercular agent isoniazid. Indeed, it has been estimated that over 70% of isoniazid resistant Mtb carry mutations that render KatG unable to catalyze isoniazid activation. Second, KatG is prominently distributed among some of the planet’s most notorious pathogenic organisms where its production is often connected with other virulence factors. This is true for both bacterial pathogens (e.g., the organisms that causes of tuberculosis and bubonic plague) and fungal pathogens (e.g., the organism that causes rice blast disease). This perhaps should not be too surprising given that a near universal response of higher eukaryotes (the intended hosts for these pathogens) is to produce large amounts of H2O2 to defend against infection.
The Goodwin laboratory has observed that peroxidatic electron donors (PxEDs) do not inhibit catalase activity as the entire field had anticipated, rather they stimulate catalase activity by at least an order of magnitude. PxED’s not only increase the efficiency of H2O2 degradation, but they also dramatically expand the pH range over which rapid H2O2 degradation can be expected. This new pH range matches precisely the conditions that infected hosts use to defend themselves against pathogens like those mentioned above. As we have investigated this phenomenon, we have uncovered that the PxED stimulatory effect and most aspects of KatG catalysis are connected to how the enzyme controls through-protein electron transfer. This has led to an NSF-funded project to evaluate intramolecular electron transfer as it relates to posttranslational formation of KatG’s novel MYW cofactor as well as how that cofactor is used for a completely novel mechanism of H2O2 degradation.
In addition, KatGs afford a novel opportunity for making advances in enzyme engineering, providing a platform for the development of new catalysts to address specific threats to human health. For enzyme engineering to be successful, it is essential that we understand the ways in which protein structures external to an active site can be used to modulate the function of that active site. KatGs are unique in that they use a single active site for two distinct catalytic activities: catalase and peroxidase. Amino acid sequence and protein structure comparisons reveal that KatGs and monofunctional peroxidases have highly similar active sites. However, the monofunctional peroxidases lack appreciable catalase activity. Sequence and structural analyses also reveal the presence of three large structures in KatGs that are absent from monofunctional peroxidases: two interhelical insertions and a C-terminal domain. All three of these features are peripheral to the active site. Thus, the KatGs represent an ideal opportunity to evaluate the mechanisms of active site modulation by peripheral protein structures. Consequently, our research holds great promise for making necessary advances to support efforts in enzyme engineering.
Identifying natural product inhibitors of M. tuberculosis shikimate kinase. As mentioned above, drug-resistant Mtb continues to pose a substantial threat to human health. Alarmingly, the FDA has only approved one new antitubercular agent since the 1960’s. Clearly, the need for new drugs to treat Mtb is pressing. Collaborating with Dr. Angela Calderón in the Drug Discovery and Development, we are investigating the shikimate pathway as a potential target for new antitubercular agents, and we are drawing on natural products as a source for new scaffolds for the development of such compounds. The shikimate pathway is particularly attractive for drug targets because it is essential for mycobacterial survival, but it is not present in humans. We are currently identifying natural product inhibitors for shikimate kinase. We are using mass spectrometry based rapid screening approaches to identify inhibitors, but it is not enough to simply identify such compounds. The compounds most likely to be successful as leads for new antitubercular agents must be mechanistically appropriate. That is, they must inhibit the aspects of the mechanism associated with shikimate (not present in human metabolism) but not those aspects of the mechanism associated with ATP (widely distributed in human metabolism). We are using site-directed mutagenesis to produce a panel of Mtb shikimate kinase variants for targeted intrinsic protein fluorescence studies. By selectively introducing tryptophan and by extension unique intrinsic fluorescent properties in each variant, we will have an approach to rapidly screen inhibitors for their binding properties including those aspects of the enzyme’s mechanism with which they interfere.
4.B.b.1. Peer-Reviewed Journal Articles:
(from Google Scholar: h-index = 23; i10 index = 34; total
citations = 2608)
(Citations as
of 07/29/2023; unless otherwise indicated, 2023 Impact Factors [2020 IF] are
shown)
(For all
Auburn-based output, *denotes graduate student coauthor; ** denotes
undergraduate coauthor)
Resulting from research at
Auburn University after tenure
42. Li, J., Duan, R.,
Traore, E. S., Davis, I., Nguyen, R. C., Goodwin, D. C., Lamb, A., Jarzecki, A. A., Liu, A., Discovery and
characterization of a catalase-dormant form of Mycobacterium
tuberculosis KatG with a Met-Tyr-Trp-OOH
cofactor. In preparation.
41. *Alam, J., *Olofintila, O. E., *Moen, F. S., Noel, Z. A., Liles, M. R., and Goodwin, D. C.
2022. Broad antibiosis activity of Bacillus velezensis and Bacillus subtilis is accounted
for by a conserved capacity for lipopeptide biosynthesis. Frontiers Microbiol. (submitted
July 28, 2023).
40. de Faria, C. F.,
Moreira, T., Lopes, P., Costa, H., *Krewall, J. R., *Barton,
C. M., Santos, S., Goodwin, D. C., Mochado, D., Viveiros, M., Machuqueiro, M., and
Martins, F. 2021. Designing new antitubercular isoniazid derivatives with
improved reactivity and membrane trafficking abilities. Biomed.
Pharmacother. 144, 112362. (2023 IF: 7.419; Times
Cited: 11; Goodwin Laboratory Contribution: 20%.)
39. *Basak, S., *Alam, J., Goodwin, D., Harris, J., Patel, J.D., McCullough, P., and McElroy, J.S. 2022. Detecting ACCase-targeting herbicides effect on ACCase activity utilizing a malachite green colorimetric functional assay Weed Sci., 70, 14 – 19. (2023 IF: 2.58; Times Cited: 1; Goodwin Laboratory Contribution: 20%.)
38. **Sahrmann, P.G., *Donnan, P.H., Merz, K.M. Mansoorabadi, S.O., and Goodwin, D.C. 2020. MRP.py: A parameterizer of post-translationally modified residues. J. Chem. Inf. Model. 60, 4424-4428. (2023 IF: 5.60; Times Cited: 1)
37. *Simithy,
J., *Fuanta, N.R., *Alturki,
M., Hobrath, J.V., Wahba, A.E., Pina, I., Rath, J.,
Hamann, M.T., DeRuiter, J., Goodwin, D.C., and
Calderón, A.I. 2018. Slow-binding inhibition of Mycobacterium tuberculosis shikimate kinase by manzamine alkaloids.
Biochemistry 52, 4923 - 4933. (2023
IF: 3.321; Times Cited: 27; Goodwin Laboratory Contribution: 40%; Simithy [Calderón lab] and Fuanta
[Goodwin lab] are noted to have contributed equally to the work.)
36. *Simithy, J., *Fuanta, N.R., Hobrath, J.V., Kochanowska-Karamayan, A., Hamann, M.T., Goodwin, D.C., and Calderón, A.I. 2018. Mechanism of irreversible inhibition of Mycobacterium tuberculosis shikimate kinase by ilimaquinone. Biochim. Biophys. Acta 1866, 731 – 739. (2023 IF: 4.125; Times Cited: 12; Goodwin Laboratory Contribution: 40%; Simithy [Calderón lab] and Fuanta [Goodwin lab] are noted to have contributed equally to the work.)
35. *Alturki, M.S., *Fuanta, N.R., **Jarrard, M.A., Hobrath, J.V., Goodwin, D.C., *Rants’o, T.A., and Calderón, A.I. 2018. A multifaceted approach to identify non-specific enzyme inhibition: Application to Mycobacterium tuberculosis shikimate kinase. Bioorg. Medicin. Chem. Lett. 28, 802 – 808. (2023 IF: 2.940; Times Cited: 8; Goodwin Laboratory Contribution: 20%)
34. *Njuma, O.J., Davis, I., *Ndontsa, E.N., *Krewall, J.R., Liu, A., and Goodwin, D.C. 2017. Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron-hole hopping within the enzyme. J. Biol. Chem. 292, 18408 – 18421. (2023 IF: 5.485; Times Cited: 18; Goodwin Laboratory Contribution: 75%)
33. **McCarty, S.E., **Schellenberger, A., Goodwin, D.C., *Fuanta, N.R., Tekwani, B.L., and Calderón, A.I. 2015. Plasmodium falciparum thioredoxin reductase (PfTrxR) and its role as a target for antimalarial discovery. Molecules 20, 11459 – 73. (2023 IF: 4.927; Times Cited: 19; Goodwin Laboratory Contribution: 35%)
32. *Huang, J., Smith,
F., Panizzi, J.R., Goodwin, D.C., and Panizzi, P. 2015. Inactivation of myeloperoxidase by
benzoic acid hydrazide. Arch. Biochem. Biophys. 570, 14 –
22. (2023 IF: 3.391; Times Cited: 20; Goodwin Laboratory Contribution: 10%)
31. *Kudalkar, S., *Li, Y., **Muldowney, M., and Goodwin, D.C. 2015. A role for catalase-peroxidase large loop 2 revealed by deletion mutagenesis: Control of active site water and ferric enzyme reactivity. Biochemistry 54, 1648 - 1662. (2023 IF: 3.321; Times Cited: 7; Goodwin Laboratory Contribution: 100%)
30. **Gordon, S., *Simithy, J., Goodwin, D.C., and Calderón, A.I. 2015. Selective Mycobacterium tuberculosis shikimate kinase inhibitors as potential antibacterials. Perspec. Med. Chem. 7, 9 – 20. (Times Cited: 32; Goodwin Laboratory Contribution: 25%)
29. *Simithy, J., **Gill, G., *Wang, Y., Goodwin, D.C., and Calderón, A.I. 2015. Development of an ESI-LC-MS-based assay for kinetic evaluation of M. tuberculosis shikimate kinase activity and inhibition. Anal. Chem. 87, 2129 – 2136. (2023 IF: 8.008; Times Cited: 13; Goodwin Laboratory Contribution: 50%)
28. *Njuma, O.J., *Ndontsa, E.N., and Goodwin D.C. 2014. Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG. Arch. Biochem. Biophys. 544, 27 – 39. (2023 IF: 3.391; Times Cited: 46; Goodwin Laboratory Contribution: 100%)
27. *Wang, Y., and Goodwin, D.C. 2013. Integral role of the I*-helix in the function of the inactive C-terminal domain of catalase-peroxidase (KatG). Biochim. Biophys. Acta 1834, 362 – 371. (2023 IF: 4.125; Times Cited: 9; Goodwin Laboratory Contribution: 100%)
26. *Kudalkar, S.N., **Campbell, R.A., *Li, Y., *Varnado, C.L., **Prescott, C., and Goodwin, D.C. 2012. Enhancing peroxidatic turnover of KatG by deletion mutagenesis. J. Inorg. Biochem. 116, 106 – 115. (2023 IF: 4.336; Times Cited: 14; Goodwin Laboratory Contribution: 100%)
25. *Ndontsa, E.N., *Moore, R.L., and Goodwin, D.C. 2012. Stimulation of KatG catalase activity by peroxidatic electron donors. Arch. Biochem. Biophys. 525, 215 – 222. (2023 IF: 3.391; Times Cited: 19; Goodwin Laboratory Contribution: 100%)
24. Tejero, J.,
Biswas, A., Haque, M.M., Wang, Z.Q., Hemann, C., *Varnado,
C.L., Hille, R., Goodwin, D.C., and Stuehr, D.J.
2011. Mesohaem
substitution reveals how haem electronic properties
can influence the kinetic and catalytic parameters of neuronal NO
synthase. Biochem. J. 433, 163 – 174. (2023
IF: 3.766; Times Cited: 11; Goodwin Laboratory Contribution: 10%)
23. *Moore, R.L., *Cook, C.O., **Williams, R.,
and Goodwin, D.C. 2008. Substitution of strictly
conserved Y111 in catalase-peroxidase:
Impact of remote interdomain contacts on active site structure and
catalytic performance. J. Inorg. Biochem. 102, 1819 – 1824. (2023 IF: 4.336;
Times Cited: 5; Goodwin Laboratory Contribution: 100%)
22. *Moore, R.L., **Powell, L.J., and Goodwin, D.C. 2008. The kinetic properties producing the perfunctory pH profiles of catalase-peroxidases. Biochim. Biophys. Acta. 1784, 900 – 907. (2020 IF: 4.125; Times Cited: 19; Goodwin Laboratory Contribution: 100%)
21. *Baker, R.D., *Cook, C.O., and Goodwin, D.C. 2006. Catalase-peroxidase active site restructuring by a distant an inactive domain. Biochemistry 45, 7113-7121. (2023 IF: 3.321; Times Cited: 25; Goodwin Laboratory Contribution: 100%)
Resulting from research at Auburn University before tenure
20. *Baker, R.D., *Cook, C.O., and Goodwin, D.C. 2004.
Properties of catalase-peroxidase lacking its C-terminal domain. Biochem. Biophys. Res.
Comm. 320, 833-839. (2023 IF: 3.10; Times Cited: 44; Goodwin Laboratory
Contribution: 100%)
19. *Li, Y., and Goodwin, D.C. 2004. Vital roles of an interhelical insertion in catalase-peroxidase bifunctionality. Biochem. Biophys. Res. Comm. 318, 970-976. (2023 IF: 3.10; Times Cited: 24; Goodwin Laboratory Contribution: 100%)
18. *Varnado, C.L., and Goodwin, D.C. 2004. System for the expression of recombinant hemoproteins in Escherichia coli. Prot. Exp. Purif. 35, 76-83. (2023 IF: 2.025; Times Cited: 73; Goodwin Laboratory Contribution: 100%)
17. *Varnado, C.L., **Hertwig, K.M., **Thomas, R., **Roberts, J.K., and Goodwin,
D.C. 2004. Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7. Arch. Biochem. Biophys. 421,
166-174. (2020 IF: 3.391; Times Cited: 48; Goodwin Laboratory Contribution:
100%)
16. Goodwin, D.C., and **Hertwig, K. M. 2003.
Peroxidase-catalyzed oxidation of capsaicinoids: Steady-state and transient-state kinetic
studies. Arch. Biochem. Biophys.
417, 18-26. (2020 IF: 3.391; Times Cited: 38; Goodwin Laboratory Contribution:
100%)
Publications resulting from research before coming to Auburn University
15. Trostchansky, A., O-Donnell, V.B., Goodwin, D.C., Landino, L.M., Marnett, L.J., Radi, R., and Rubbo, H. 2007. PGHS-1 in turnover is inactivated by peroxynitrite derived- radicals: Differential effect of .NO on peroxidase and cyclooxygenase activities. Free Rad. Biol. Med. 41, 1029 – 1038. (2023 IF: 8.101; Times Cited: 47)
14. Goodwin, D.C., Rowlinson,
S.W., and Marnett, L.J. 2000.
Substitution of tyrosine for the proximal histidine ligand to the heme
of prostaglandin endoperoxide synthase-2:
Implications for the mechanism of cyclooxygenase activation and
catalysis. Biochemistry 39,
5422-5432. (2023 IF: 3.321; Times Cited: 24; Times Cited: 53)
13. Kiefer, J.R., Pawlitz, J.L., Moreland, K.T., Stegeman, R.A., Hood, W.F., Gierse, J.K., Stevens, A.M., Goodwin, D.C., Rowlinson, S.W., Marnett, L.J., Stallings, W.C., and Kurumbail, R.G. 2000. Structural insights into the stereochemistry of the cyclooxygenase reaction. Nature 405, 97-101. (2023 IF: 69.504; Times Cited: 279)
12. Rowlinson, S.W.,
Crews, B.C., Gierse, J.K., Goodwin, D.C. and Marnett, L.J. 2000.
Spatial requirements for 15-HETE synthesis within the cyclooxygenase
active site of murine COX-2: why
acetylated COX-1 does not synthesize 15-R-HETE.
J. Biol. Chem. 275, 6586-6591. (2023 IF: 5.485; Times Cited: 97)
11. Goodwin, D.C., Landino, L.M., and Marnett, L.J. 1999. Effects of nitric oxide and nitric oxide-derived species on prostaglandin endoperoxide synthase and prostaglandin biosynthesis. FASEB J. 13, 1121-1136. (2023 IF: 5.834; Times Cited: 221)
10. Goodwin, D.C., Landino, L.M., and Marnett, L.J. 1999. Reactions of prostaglandin endoperoxide synthase with nitric oxide and peroxynitrite. Drug Metabolism Reviews 31, 273-294. (2023 IF: 6.984; Times Cited: 29)
9. Marnett, L.J., Rowlinson, S.W.,
Goodwin, D.C., Kalgutkar, A.S., and Lanzo, C.A. 1999.
Arachidonic acid oxygenation by COX-1 and COX-2: Mechanisms of catalysis and
inhibition. J. Biol. Chem. 274, 22903-22906. (2023 IF: 5.485; Times Cited: 683)
8. Goodwin,
D.C., Gunther, M.R., Hsi, L.C., Crews, B.C., Eling, T.E., Mason, R.P., and Marnett,
L.J. 1998. Nitric oxide trapping of tyrosyl radicals
generated during prostaglandin endoperoxide synthase turnover: detection of the
radical derivative of tyrosine 385. J.
Biol. Chem. 273, 8903-8909. (2023
IF: 5.485; Times Cited: 164)
7. Goodwin, D.C., Grover, T.A., and Aust, S.D. 1997.
Roles of efficient substrates in peroxidase-catalyzed oxidations. Biochemistry 36, 139-147. (2023 IF: 3.321; Times Cited: 54)
6. Goodwin,
D.C., Grover, T.A., and Aust, S.D.
1996. Redox mediation in the
peroxidase-catalyzed oxidation of aminopyrine: possible implications for
drug-drug interactions. Chem. Res. Toxicol. 9,
476-483. (2020 IF: 3.739; Times Cited: 33)
5. Goodwin,
D. C., Aust, S. D., and Grover, T. A.
1996. Free radicals produced
during oxidation of hydrazines by hypochlorous
acid. Chem. Res. Toxicol. 9, 1333-1339. (2023 IF: 3.973; Times Cited: 30)
4. Goodwin,
D.C., Aust, S.D., and Grover, T.A. 1995.
Evidence for veratryl alcohol as a redox
mediator in lignin peroxidase-catalyzed oxidation. Biochemistry
34, 5060-5065. (2023 IF: 3.973;
Times Cited: 105)
3. Goodwin, D.C., Yamazaki, I., Aust, S.D., and
Grover, T.A. 1995. Determination of transient-state rate
constants for rapid peroxidase reactions. Anal.
Biochem. 231,
333-338. (2020 IF: 3.191; Times Cited: 44)
2. Goodwin,
D.C., Barr, D. P., Aust, S. D., and Grover, T. A. 1994.
The role of oxalate in lignin peroxidase catalyzed reduction: Protection
from compound III accumulation. Arch. Biochem. Biophys. 315:
267-272. (2020 IF: 3.931; Times Cited: 16)
1. Goodwin,
D.C., and Lee, S. B. 1993. Rapid, microwave mini-prep of total genomic
DNA from fungi, plants, protists and animals for PCR. BioTechniques 15:
438- 444. (2016 IF: 2.746; Times Cited: 199)
4.B.b.2 Peer-Reviewed Book Chapters:
Resulting from research after coming to
Auburn University
3. *Krewall,
J.R., **Minton, L.E., and Goodwin, D.C. 2020. KatG
structure and mechanism: Using protein-based oxidation to confront the threats
of reactive oxygen. In Bridging
Structure and Function in Mechanistic Enzymology. J. M. Miller, Ed. ACS
Symposium Series, 1357, 83-120. (Goodwin Laboratory Contribution: 100%)
2. Goodwin, D.C., **Laband, K.L., and **Hertwig, K.M. 2005. Transient- and steady-state kinetics of peroxidase-catalyzed capsaicinoid oxidation. In Phenolics in Foods and Natural Health Products. C. T. Ho and F. Shahidi, Eds. ACS Symposium Series, 909, 161-174. (Goodwin Laboratory Contribution: 100%)
Resulting from research before coming to Auburn University
1. Marnett, L.J., D.C. Goodwin, S.W. Rowlinson, A.S. Kalgutkar, and L.M. Landino. 1999. Structure, function, and inhibition of prostaglandin endoperoxide synthase. In Comprehensive Natural Products Chemistry, Vol. V pp. 225-261. C.D. Poulter, Ed. Elsevier Science, Amsterdam.
4.B.b.3. Conference Proceedings:
Resulting from research after coming to
Auburn University
1. *Cook, C.O., *Moore, R.L., and Goodwin, D.C.
2008. The effect of R117 and D597 interdomain residue substitutions on the
reactivation of Escherichia coli
catalase-peroxidase. NOBCChE Proceedings: 35th Annual National Conference. (Goodwin Laboratory Contribution:
100%)
4.B.c. Presented
Papers and Lectures
4.B.c.1. Invited Presentations (University Departments):
(† denotes
the presenter, oral if underlined; * denotes graduate student coauthor; **
denotes undergraduate coauthor)
Resulting from research after coming to
Auburn University
28. †Goodwin, D. C. “Radicals and Switches: Synergy or Antagonism in the Operation of a Bifunctional Enzyme?” Department of Chemistry, LaGrange College, March 21, 2016.
27. †Goodwin, D. C. “Tryptophanyl Radicals and Arginine Switches: Synergy or Antagonism in the Operation of a Bifunctional Enzyme?” Department of Chemistry and Biochemistry, University of North Georgia, February 5, 2016.
26. †Goodwin, D. C. “Tryptophanyl Radicals and Arginine Switches: Synergy or Antagonism in the Operation of a Bifunctional Enzyme?” Department of Chemistry, Kansas State University, January 28, 2016.
25. †*Njuma, O. J.,
Davis, I., *Ndontsa,
E. N.,
Liu, A., and Goodwin, D.C. “Electron donors to the rescue: The proximal
tryptophan as a potential conduit for catalase-peroxidase inactivation.”
Department of Chemistry, University of Buea, Cameroon. April 1, 2015.
24. †Goodwin, D.C. “Novel Mechanisms for Hydrogen Peroxide Degradation Catalyzed by KatG: Implications for Antibiotic Resistance and Bacterial Virulence.” Department of Chemistry and Biochemistry, Kennesaw State University, October 3, 2012.
23. †Goodwin, D. C. “The transformation of enzyme function: Commandeering an old framework for new activity.” Department of Chemistry, University of South Alabama, September 10, 2010.
22. †Goodwin, D. C. “Structural requirements for the hemoprotein-dependent decomposition of hydroperoxides: Lessons from the catalase-peroxidases.” Department of Chemistry, Georgia State University, March 20, 2009.
21. †Goodwin,
D. C. “Structures and Mechanisms of
Hemoproteins: Implications for Enzyme
Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of
Chemistry, Jacksonville State University, February 20, 2007.
20. †Goodwin,
D. C.
“Contribution of Protein Structural Features to the Unique Catalytic Properties
of Catalase-Peroxidases: Implications
for Bacterial Virulence, Antibiotic Resistance, and Enzyme Engineering.”
Department of Chemistry and Physics, Georgia College and State University,
Milledgeville, GA, February 2006.
19. †Goodwin,
D. C.
“Contribution of Protein Structural Features to the Unique Catalytic Properties
of Catalase-Peroxidases: Implications
for Bacterial Virulence, Antibiotic Resistance, and Enzyme Engineering.”
Department of Chemistry, University of West Florida, Pensacola, FL, October 21,
2005.
18. †Goodwin, D. C. “Protein
Structural Contributions to the Unique Catalytic Properties of
Catalase-Peroxidases.” Department of Chemistry and
Biochemistry, University of Delaware, Newark, DE, November 1, 2004.
17. †Goodwin, D. C. “Protein
Structural Contributions to the Unique Catalytic Properties of
Catalase-Peroxidases.” Department of Biochemistry,
Wake Forest University, Winston-Salem, NC, August 3, 2004.
16. †Goodwin,
D. C. “Protein Structural Contributions to the Unique Catalytic Properties
of Catalase-Peroxidases.” Department of Chemistry,
New York University, New York, NY, April 26, 2004.
15. †Goodwin, D. C.
“Structural Requirements for the Hemoprotein-Dependent Decomposition of
Hydroperoxides: Lessons from the
Catalase-Peroxidases.” Department of Biochemistry, Vanderbilt University,
Nashville, TN, March 26, 2004.
14. †Goodwin,
D. C. “Hemoprotein Structure and Mechanism: Implications for Enzyme
Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of Chemistry and Physics, LaGrange College, LaGrange,
GA, March 10, 2004.
13. †Goodwin, D. C.
“Structural Requirements for the Hemoprotein-Dependent Decomposition of
Hydroperoxides: Lessons from the
Catalase-Peroxidases.” Department of Chemistry, Butler University,
Indianapolis, IN, February 18, 2004.
12. †Goodwin, D. C.
“Structural Requirements for the Hemoprotein-Dependent Decomposition of
Hydroperoxides: Lessons from the
Catalase-Peroxidases.” Department of Chemistry, Case Western Reserve
University, Cleveland, OH, February 6, 2004.
11. †Goodwin, D. C. “Hemoprotein Structure and Mechanism: Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of Chemistry and Physics, Georgia College and State University, Milledgeville, GA, February 2, 2004.
10. †Goodwin
D. C. “Hemoprotein Structure and Mechanism:
Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic
Resistance.” Department of Chemistry,
State University of West Georgia, Carrollton, GA, April 11, 2003.
9. †Goodwin,
D. C. “Hemoprotein Structure and Mechanism:
Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic
Resistance.” Department of Chemistry, University of Mississippi, Oxford, MS,
October 18, 2002.
8. †Goodwin, D. C. “Catalase/Peroxidase Structure, Function, and Kinetics: Implications for Antibiotic Resistance and Bacterial Virulence.” Department of Chemistry, State University of West Georgia, Carollton, GA. April 27, 2000.
7. †Goodwin,
D. C. “Mechanisms of Prostaglandin
Biosynthesis: Generation and Trapping of
Tyrosyl Radicals.” Department of Chemistry and Biochemistry, University of
Texas at Arlington, Arlington, TX. April
26, 1999.
6. †Goodwin, D. C. “Structure and
Function of Catalase/Peroxidases:
Implications for Antibiotic Resistance and Virulence.” Department of
Chemistry and Biochemistry, University of Texas at Arlington, Arlington,
TX. April 27, 1999.
Resulting
from research before coming to Auburn University
5.
†Goodwin, D.C. “Mechanisms of Prostaglandin
Biosynthesis: Generation and Trapping of
Tyrosyl Radicals.” Department of Chemistry, Auburn University, Auburn, AL. January 29, 1999.
4. †Goodwin, D.C.
“Structure and Function of Catalase/Peroxidases: Implications for Antibiotic
Resistance and Virulence.” Department of Chemistry, Auburn University, Auburn,
AL. April 26, 1999.
3. †Goodwin, D.C. “Kinetics of redox mediation in
peroxidase catalysis: implications for
metabolism of xenobiotics.” Department
of Biochemistry, Center in Molecular Toxicology, School of Medicine, Vanderbilt
University, Nashville, TN. April 2, 1996.
2. †Goodwin, D.C. “Kinetics of redox mediation in
peroxidase catalysis: implications for
metabolism of xenobiotics.”
Atherosclerosis, Nutrition, and Lipid Research Division, School of
Medicine, Washington University, Saint Louis, MO, April 4, 1996.
1. †Goodwin, D.C. “Kinetics of redox mediation in
peroxidase catalysis: implications for
metabolism of xenobiotics.” Department
of Biochemistry, Michigan State University, East Lansing, MI, April 8, 1996.
4.B.c.2. Invited Presentations (Conferences):
(† denotes
the presenter, oral if underlined; * denotes graduate student coauthor; **
denotes undergraduate coauthor)
Resulting
from research after coming to Auburn University
6. †Goodwin, D.C. “Radicals, switches, and a protein-based cofactor: Expanding
the catalytic abilities of an old active site.”
Advancements in Mechanistic Enzymology;
SERMACS 2019, Savannah, GA, October 21, 2019.
5. †Goodwin,
D.C. “Intramolecular electron
transfer for self-preservation and bifunctional catalysis.” Gordon Research Conference: Enzymes,
Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 23, 2018.
4. †Goodwin,
D.C. “Intramolecular radical
transfer: How KatG enlists self-preservation for
synergistic bifunctional catalysis.” Session:
Bioinorganic Chemistry in the Southeast: From Small Molecules to
Macromolecules. SERMACS 2017, Charlotte, NC, November 8 2017.
3. †Goodwin, D.C., *Baker, R.D., *Cook, C.O., and **Laband,
K. A. “Integral Involvement of an Inactive Domain in Catalase-Peroxidase
Structure and Catalysis.” Gordon Conference: Enzymes, Coenzymes, and
Metabolic Pathways, Meriden, NH, July 20, 2004.
2. †Goodwin, D.C., *Baker, R.D., *Varnado, C.L., and *Li,Y. “Structural
Requirements for the Hemoprotein-Dependent Decomposition of
Hydroperoxides: Lessons from the
Catalase-Peroxidases.” Symposium Title: Chemistry and Biology of Oxidative
Damage. Southeast Regional Meeting of
the American Chemical Society, Atlanta, GA, November 5, 2003.
4.B.c.3. Presentations from submitted and accepted abstracts:
(† denotes
the presenter, oral if underlined; * denotes graduate student coauthor; **
denotes undergraduate coauthor)
Resulting from research after
coming to Auburn University
117. †*Ugochukwu, C. G., Schwartz, T.
S., Ellis, H. R., and Goodwin, D. C. “Sulfur starvation induces Fe-replete
response and attenuates virulence pathways in Pseudomonas aeruginosa PAO1.” American Society for
Microbiology Microbe, Houston, TX, June 17, 2023.
116. †*Ugochukwu, C. G., Schwartz, T.
S., Ellis, H. R., and Goodwin, D. C. “Sulfur starvation induces Fe-replete
response and attenuates virulence pathways in Pseudomonas aeruginosa PAO1.” 13th Annual Southeast Enzyme Conference, Atlanta, GA, April
22, 2023.
115. †*Islam,
R., and Goodwin, D. C. “Shikimate pathway enzymes as candidates for multitarget
inhibitor development.” 13th Annual Southeast Enzyme Conference,
Atlanta, GA, April 22, 2023.
114. †*Alam, M. J., Liles, M. R., McInroy, J. A., Noel, Z. A., and Goodwin,
D. C. “Structural and functional insights of Bacillus cytochromes P450
that are involved in secondar metabolite biosynthesis.” 12th Annual
Southeast Enzyme Conference Atlanta,
GA, April 23, 2022.
113. †*Aziz, T., **Ryan Mumford, and Goodwin, D. C. “Mechanistic
insight into the initiation step of Methionine-Tyrosine-Tryptophan (MYW) Adduct
in Mycobacterium tuberculosis KatG.” American
Society for Biochemistry and Molecular Biology (ASBMB), Philadelphia, PA, April
4, 2022.
112. †*Aziz, T. and
Goodwin, D. C. “Partial Formation of a Protein-based Cofactor in M.
tuberculosis KatG and Its Impact on Catalysis.” Southeast
Regional Meeting of the American Chemical Society (SERMACS), Birmingham,
AL, November 12, 2021.
111. †*Alam, M. J., Liles,
M. R., McInroy, J. A., Noel, Z. A., and Goodwin, D. C. “Bacillus Secondary Metabolites as Potential Biocontrol Agents Against Plant
Pathogenic Oomycetes.” Plant
Health 2021 Online, American Phytopathological Society, Virtual, August 4, 2021.
110. †*Aziz, T. and Goodwin, D. C. “New
Insight into the Protein-based Cofactor of Mycobacterium tuberculosis KatG: Toward Better Understanding an Unusual Catalase
Mechanism.” Experimental Biology 2021, Virtual,
April 28, 2021.
109. †*Alam, M. J.
and Goodwin, D. C. “Properties of a
CYP102A2 predicted to participate in plantazolicin
biosynthesis.” 11th
Southeast Enzyme Conference, Virtual, April 10, 2021.
108. †**Lee, A. K., *Barton, C. M., *Krewall, J. R., **Petrus, S., and Goodwin, D. C. “Evaluating the function of tryptophans near KatG’s
heme-dependent active site.” 11th
Southeast Enzyme Conference, Virtual, April 10, 2021.
107. †**Forbes, M., *Krewall, J. R., **Minton, L. E., and Goodwin, D. C. “An Arg switch and the formation of a protein-based cofactor in catalase-peroxidase (KatG).” 11th Southeast Enzyme Conference, Virtual, April 10, 2021.
106. †*Basak,
S., *Alam, M. J., McElroy, J. S., and Goodwin, D. C.
“Effects of ACCase-targeting
herbicides on the detection of southern crabgrass resistance using the
malachite green colorimetric assay.” 11th
Southeast Enzyme Conference, Virtual, April 10, 2021.
105. †**Lee, A. K., **Petrus, S., *Krewall, J. R., *Barton,
C. M., and Goodwin, D. C. “Impact of heme incorporation procedure on
intermediates of KatG reaction with peroxides.” 52nd Southeastern Undergraduate
Research Conference, Tuscaloosa, AL, January 25, 2020.
104. †**Minton, L. E., *Xu, H., *Krewall, J. R., *Barton,
C. M., and Goodwin, D. C. “Impact of heme incorporation procedure on
intermediates of KatG reaction with peroxides.” 52nd Southeastern Undergraduate
Research Conference, Tuscaloosa, AL, January 25, 2020. (Received a poster award).
103. *Aziz,
T., *Barton, C. M., *Krewall, J. R., *Xu, H.,
and †Goodwin, D. C. “Toward
identification of intermediates in the formation of a novel protein-based
cofactor” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 21 - 27, 2019.
102. †*Krewall,
J. R., **Sahrmann, P. G., and Goodwin, D. C. “Elucidating
the novel features of the catalase mechanism of catalase-peroxidases” Gordon
Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 21 - 27, 2019.
101. †**Sahrmann,
P. G., *Donnan, P. H., *Krewall, J. R., and Goodwin, D. C. “Charged side chains
enable KatG active site gatekeeping: A computational
investigation of a peroxide-degrading enzyme.” 10th Annual Southeast Enzyme Conference, Atlanta, GA,
Atlanta, GA, April 13, 2019.
100. †*Aziz, T., †*Barton, C. M., and Goodwin, D. C. “Impact of
heme incorporation procedure on intermediates of KatG
reaction with peroxides.” 10th
Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 13, 2019.
99. †**McWhorter,
K., *Xu, H., and Goodwin, D. C. “Use of multiple active-site tryptophans to direct off-catalase electron transfer and
sustain the activity of a peroxide-detoxifying enzyme.” Southeast Regional Meeting of American Chemical Society (SERMACS),
Augusta, GA, November 2, 2018.
98. †**McWhorter,
K., *Xu, H., and Goodwin, D. C. “Tryptophans in
tandem: How to sustain KatG catalase activity with peroxidatic electron donors.” Herty Medal Undergraduate Research Symposium 2018, Lawrenceville, GA,
September 21, 2018.
97. †*Krewall, J. R., *Njuma, O. J., **Sahrmann, P., and Goodwin, D. C. “How intraprotein radical transfer and the role-reversal of heme intermediates generate a unique catalase mechanism.” 9th Annual Southeast Enzyme Conference, Atlanta, GA, April 7, 2018.
96. †*Xu, H., *Njuma, O., and Goodwin, D.C. “How an arginine switch promotes the self-preservation of an H2O2-degrading enzyme.” 9th Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 7, 2018.
95. †**McWhorter, K.L., *Xu, H., and Goodwin, D.C. “Exploiting active-site tryptophans to direct off-mechanism electron transfer: Preserving the activity of peroxide-detoxifying enzymes.” 9th Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 7, 2018.
94. †**Sahrmann, P., **McWhorter, K. L., *Krewall, J. R., and Goodwin, D. C. “Electron-hole hopping as catalytic self-preservation: How catalase-peroxidase from M. tuberculosis avoids the perils of peroxide decomposition.” 9th Annual Southeast Enzyme Conference Atlanta, GA, Atlanta, GA, April 7, 2018.
93. †*Fuanta, N. R., *Simithy, J., **Skinner, M., **Gill, G., **Childers, T., Calderón, A. I., and Goodwin D. “An approach towards rapid inhibitor screening and mechanistic evaluation of tuberculosis shikimate kinase: intrinsic and extrinsic fluorescence.” National Meeting of the National Organization for the Professional Advancement of Black Chemist and Chemical Engineers (NOBCChE), Minneapolis, MN, October 2017.
92. †*Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “Role reversal between peroxidase reaction intermediates generates the distinct catalase mechanism of catalase-peroxidase.” 46th Annual Southeast Magnetic Resonance Conference, Tallahassee, FL, October 21, 2017.
91. †*Xu, H., *Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer.” 46th Annual Southeast Magnetic Resonance Conference, Tallahassee, FL, October 21, 2017.
90. †*Fuanta, R., *Simithy, J., **Skinner, M., **Gill, G., **Childers,
T., Calderón, A. I., and Goodwin D.
“Imparting intrinsic flourescence
as an approach towards rapid inhibitor screening and mechanistic evaluation of
tuberculosis shikimate kinase.” 254th
National Meeting of the American
Chemical Society, Washington D.C, August 2017.
89. *Xu, H., *Krewall, J.
R., *Njuma, O. J., Davis, I., Liu, A., and †*Goodwin,
D. C. “Using an arginine switch and an active site tryptophan to direct
off-pathway electron transfer: Maximizing catalase activity from a peroxidase
scaffold.” Gordon Research Conference:
Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 16
– 21, 2017.
88. †*Krewall, J. R., *Xu, H., *Njuma, O. J., and Goodwin, D. C. “Directing off-pathway protein oxidation to preserve enzyme activity: At last, a role for the proximal tryptophan of KatG.” 7th Annual Lester Andrews Symposium, Starkville, MS, May 31, 2017.
87. †*Xu, H., *Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer.” 7th Annual Lester Andrews Symposium, Starkville, MS, May 31, 2017.
86. †*Krewall, J. R., *Xu, H., *Njuma, O. J., and Goodwin, D. C. “Directing off-pathway protein oxidation to preserve enzyme activity: At last, a role for the proximal tryptophan of KatG.” 8th Annual Southeast Enzyme Conference, Atlanta, GA, April 8, 2017.
85. †*Xu, H., *Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer.” 8th Annual Southeast Enzyme Conference, Atlanta, GA, April 8, 2017.
84. †*Fuanta, N. R., *Simithy, J., **Gill, G., **Kollhoff, A., **Childers, T., Calderón, A. I., and Goodwin D. “Towards high-throughput drug screening and mechanistic evaluation of tuberculosis shikimate kinase; Intrinsic protein fluorescence.” National Organization for the Professional Advancement of Black Chemist and Chemical Engineers (NOBCChE), Raleigh, NC, November 2016.
83. †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and Goodwin, D.C. “Pathways and regulation of intramolecular electron transfer in catalase-peroxidases (KatG).” BEST Symposium, DOW Chemical Company, October 1, 2016.
82. †*Fuanta, N. R., *Simithy, J., **Gill, G., **Kollhoff, A., **Childers, T., Calderón, A. I., and Goodwin D. C. “Targeted intrinsic protein fluorescence, an approach towards high-throughput drug screening and mechanistic evaluation of tuberculosis shikimate kinase.” Southeast Regional Meeting of American Chemical Society (SERMACS), Columbia, SC, October 2016.
81. †*Alturki, M. S., **Jarrard, M. A., *Fuanta, N. R.,
Goodwin, D. C., and Calderón, A. I. “LC-MS based approach to characterize
non-specific binding inhibitors to Mycobacterium
tuberculosis shikimate kinase (MtSK).” 64th
American Society for Mass Spectrometry National Conference on Mass Spectrometry
and Allied Topics, San Antonio, TX. June 5, 2016.
80. †Calderón, A. I., *Simithy, J., Goodwin, D. C., and Hamann,
M. T. “Mass spectrometry based studies on irreversible inhibition of
recombinant Mycobacterium tuberculosis
shikimate kinase by the marine sponge metabolite ilimaquinone.
64th American Society for Mass
Spectrometry National Conference on Mass Spectrometry and Allied Topics,
San Antonio, TX, June 5, 2016.
79. †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and Goodwin, D.C. “The proximal tryptophan as a potential conduit for catalase-peroxidase inactivation. 42nd National Organization for the Professional Advancement of Black Chemists and Chemical Engineers (NOBCCHE), Orlando, FL, September 21, 2015.
78. †*Njuma, O. J., Davis, I., *Ndontsa,
E. N., Liu, A., and *Goodwin, D. C. “Proximal tryptophan and arginine switch
participation in catalase-peroxidase inactivation.” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways,
Waterville Valley, NH, July 13 – 14, 2015.
77. †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and
Goodwin, D. C. 2015. Participation of the proximal tryptophan as a potential
conduit for catalase-peroxidase inactivation. 6th Annual Southeast Enzymes Conference, Georgia State
University, Atlanta, GA, April 11, 2015.
76. †*Fuanta, R., *Simithy, J., **Gill,
G., **Kollhoff, A., **Childers, T., Calderón, A. I.,
and Goodwin D. C. 2015. Site-directed
incorporation of intrinsic fluorescence in shikimate kinase to evaluate
catalysis and inhibition. 6th
Annual Southeast Enzymes Conference, Georgia State University, Atlanta, GA,
April 11, 2015.
75. †*Njuma, O. J., *Ndontsa, E. D., and Goodwin, D. C. “Evaluating the role of peroxidatic reducing substrates in an unusual catalase
activity of catalase-peroxidases.” 2014
Symposium, The Protein Society, San Diego, CA, July 27, 2014.
74. †*Simithy, J., Goodwin,
D., Hamann, M.T., and Calderón, A.I. “Evaluation of the inhibitory activity of
marine natural compounds against Mycobacterium
tuberculosis shikimate kinase (MtSK) by LC-MS.” 62nd
American Society for Mass Spectrometry Conference on Mass Spectrometry and
Allied Topics, Baltimore, MD, June 18, 2014.
73. †*Njuma, O. J., *Ndontsa, E. D., and Goodwin, D. C. “Synergistic effect of peroxidatic electron donors on the catalase activity of catalase-peroxidase.” 5th Annual Southeast Enzymes Conference, Georgia State University, Atlanta, GA, April 4, 2014.
72. †*Njuma, O. J., *Ndontsa, E. N. and Goodwin, D. C. “Evaluating the role of electron donors in a novel mechanism of H2O2 decomposition by catalase-peroxidase.” 91st Alabama Academy of Science Meeting (AAS), Auburn University, AL, March 13, 2014. (Awarded 1st Place Presentation for Chemistry Section).
71. †**McCurdy,
E., *Ndontsa, E. N., and Goodwin, D. C. “W438 and the
diminished necessity for peroxidatic rescue of KatG catalatic turnover.” 34th
Annual Undergraduate Research Conference, University of Memphis, Memphis,
TN, February 22, 2014.
70. †**McCurdy,
E., *Ndontsa, E. N., and Goodwin, D. C. “An investigation of W438 as a potential route for
off-Pathway electron transfer and its relationship to the bifunctional
activity of catalase-peroxidase.” Southeast Regional Meeting of the
American Chemical Society (SERMACS), Atlanta, GA, November 13, 2013.
(Awarded first
prize for undergraduate poster session)
69. †*Njuma, O. J., *Ndontsa, E. N., and
Goodwin, D. C. “Rescue of catalase-inactive
intermediates of KatG by peroxidatic
electron donors.” Southeast Regional Meeting of the American Chemical
Society (SERMACS), Atlanta, GA, November 13, 2013.
68. †*Njuma, O. J., *Ndontsa, E. N and Goodwin, D.C. “KatG:
Improvisation of novel peroxide decomposition mechanisms. 99th Annual
Southeastern Branch of the American Society of Microbiology Meeting
(SEBASM), Auburn University, AL, November 8, 2013.
67. †*Duan, H., Suh, S.-J., and Goodwin, D. C. “Mechanism for stimulation of bacterial defenses against H2O2 by peroxidatic electron donors.” 99th Annual Southeastern Branch of American Society of Microbiology Meeting (SEBASM), Auburn University, AL, November 8, 2013.
66. †*Njuma, O. J., *Ndontsa, E.
N., and Goodwin, D. C. “Electron donors to the rescue: Evaluating a novel
mechanism of hydrogen peroxide decomposition by catalase-peroxidases.” National
Meeting of the National
Organization
for
the Professional Advancement of Black Chemists and
Chemical Engineers (NOBCChE),
Indianapolis, IN, October 3, 2013.
65. †*Njuma, O. J., *Ndontsa, E. N., and Goodwin, D. C. “Surprising role of peroxidatic electron donors in the catalase activity of catalase-peroxidase.” Diversity Awareness Symposium, Department of Chemistry, University of Alabama, Tuscaloosa, AL, April 27, 2013. (Award-winning poster)
64. †*Ndontsa, E. N., and Goodwin D. C. “Multiple mechanisms for KatG catalase activity: Electron donors, pH, and an arginine ‘switch.’” 2012 Annual Meeting of the Southeast Region of the American Chemical Society (SERMACS), Raleigh, NC, November 14 – 17, 2012.
63. †*Ndontsa, E. N., and Goodwin, D. C. “Role of Arg 418 switch in electron-donor-enhanced catalase activity of M. tuberculosis catalase-peroxidase (KatG).” 39th Annual National Conference NOBCChE, Washington, D.C., September 24 – 28, 2012.
62. †*Ndontsa, E. N., and Goodwin, D. C. “Role of Arg 418 switch in electron-donor-enhanced catalase activity of M. tuberculosis catalase-peroxidase (KatG).” Third Southeast Enzymes Conference, Atlanta, GA,
61. †*Wang, Y., and Goodwin, D. C. “The participation of conserved I’-helix in structure, stability, and catalytic function of KatG.” Third Southeast Enzymes Conference, Atlanta, GA, April 14, 2012.
60. †*Duan, H., and Goodwin, D. “Essential role of distant interdomain interactions in H2O2 decomposition by catalase-peroxidases.” 18th Annual Meeting of the Society for Free Radical Biology and Medicine, Atlanta, GA, November 16 – 22, 2011.
59. *Wang, Y., and Goodwin, D. “Contribution of an ‘inactive’ domain to rapid H2O2 decomposition by KatG.” 18th Annual Meeting of the Society for Free Radical Biology and Medicine, Atlanta, GA, November 16 – 22, 2011.
58. †*Ndontsa, E. N., and Goodwin, D. C. “An improvised mechanism for H2O2 disproportionation based on an old enzyme scaffold.” 18th Annual Meeting of the Society for Free Radical Biology and Medicine, Atlanta, GA, November 16 – 22, 2011.
57. †*Ndontsa, E. N., and Goodwin, D. C. “An improvised mechanism for H2O2 disproportionation based on an old enzyme scaffold. Southeast/Southwest Regional Meeting, National Organization for the Professional Advancement of Black Chemists and Chemical Engineers (NOBCChE), Auburn, AL, November 11 – 12, 2011. (1st Place award winning presentation)
56. †*Kudalkar, S. N., and Goodwin, D. C. “Tracing the Impact of
a Unique Loop in Catalase-peroxidase Catalysis.” Annual Meeting of the American Society for Biochemistry and Molecular
Biology, Washington, D. C., April 9 – 13, 2011.
55. †*Kudalkar, S. N., and Goodwin, D. C. “Dependence of
catalytic ability of catalase-peroxidase on intersubunit
interactions.” Annual Meeting of the
American Society for Biochemistry and Molecular Biology, Washington, D. C.,
April 9 – 13, 2011.
54. †*Kudalkar, S. N., and Goodwin, D. C., “ Effects of progressive deletion of a unique loop on structure and function of catalase-peroxidases.” Second Southeast Enzymes Conference, Atlanta, GA, April 2, 2011.
53. †*Wang, Y., and Goodwin, D. C. “Borrowing the E. coli catalase-peroxidase C-terminal domain as a scaffold for generation of new heme-dependent catalysts.” Second Southeast Enzymes Conference, Atlanta, GA, April 2, 2011.
52. †*Ndontsa, E., and Goodwin, D. C. “Stimulation of catalase activity of catalase-peroxidases by peroxidase reducing substrates: New functions from old scaffolds.” Second Southeast Enzymes Conference, Atlanta, GA, April 2, 2011.
51. †*Goodwin, D. C., *Ndontsa, E. N., and *Moore, R. “A new role for the vestigial peroxidase function of KatG: pH-dependent catalase activation.” Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 18 – 23, 2010.
50. †*Kudalkar, S. N., and Goodwin, D. C. “Impact of intersubunit interactions on catalytic versatility of catalase-peroxidases.” First Southeast Enzyme Conference, Atlanta, GA, April 10, 2010.
49. †*Goodwin, D.C.,*Li, Y, *Kudalkar, S., **Campbell, R., and **Prescott, C. “Roles of insertional sequences in commandeering an existing enzyme framework for new catalytic function: A case study in catalase-peroxidases.” Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 5 – 10, 2009.
48. †*Moore, R. M., and
Goodwin, D. C. “ Activation of oxygen production by reducing substrates in E. coli catalase-peroxidase.” Gordon Conference: Metals in Biology, Ventura,
CA, January 25 – 30, 2009.
47. †*Cook, C.O., *Moore,
R.L., and Goodwin, D. C. “Role of R117 and D597 interdomain residues in the
reactivation of E. coli
catalase-peroxidase.” American Chemical
Society, 235th National Meeting, New Orleans, LA, April 6 – 10, 2008.
46. †*Cook, C.O.,
and Goodwin, D.C. “Role of the central hydrogen bonding network interdomain
residues in the bifunctionality of catalase-peroxidases.” NOBCChE 35th Annual Conference, Philadelphia, PA, March 17, 2008.
45. †*Cook, C.O., *Moore,
R.L., Goodwin, D.C. “Effect of distant, intradomain residues on restoring the catalase-peroxidase
bifunctional active site.” Southeast
Regional Meeting of the American Chemical Society, Greenville, SC, October
14 – 27, 2007.
44. †*Moore, R.L., **Williams,
R., and Goodwin, D.C. “Role of interdomain interaction of tyrosine 111 on
catalase-peroxidase.” Southeast Regional
Meeting of the American Chemical Society, Greenville, SC, October 14 – 27,
2007.
43. †Whitley, E.M., Goodwin, D.C., Cupp, M.S., Todd, L.W., Zhang, D., Mount, J.D., **Powell, L.J., and Cupp, E.W. 2007. “Conformational and functional stability and immunogenicity of a vasoactive insect salivary protein.” Experimental Biology Annual Meeting, Washington, DC.
42. †*Varnado, C.L., Olson, J.S., and Goodwin D.C. “Expression of recombinant hemoproteins in E. coli using a heme protein expression system.” 51st Annual Meeting of the Biophysical Society, Baltimore, MD, March 3 – 7, 2007.
41.
†*Goodwin, D.C., *Cook, C.O., *Moore,
R.L. “Roles of distant but highly conserved interactions in maintaining active
site function in catalase-peroxidases.” Gordon
Conference: Enzymes, Coenzymes, and Metabolic Pathways, Biddeford, ME, July
8 – 13, 2007.
40.
†*Cook, C. O., *Moore, R. L.,
Goodwin, D. C. “Role of intrasubunit interactions
between domains in catalase-peroxidase structure and activity.” American Chemical Society, 233rd
National Meeting, Boston, MA, August 19 – 23, 2007.
39.
†*Goodwin, D. C., *Cook, C.
O., *Baker, R. D. “Modulation of catalase-peroxidase active site structure and
catalysis by distant protein structures.” American
Chemical Society, 231st National Meeting, Atlanta, GA, March 26 – 30, 2006.
38. †*Moore, R., Goodwin, D. C., §Laband, K. A., and †Powell, L. “Role of
interdomain salt bridge on catalase-peroxidase activity.” American Chemical Society, 231st National Meeting, Atlanta, GA, March 26 – 30, 2006.
37. †*Cook, C. O., *Baker, R., and
Goodwin, D. C. “Function of a gene-duplicated domain in catalase-peroxidase
structure and activity.” American
Chemical Society, 231st National Meeting, Atlanta, GA, March 26 – 30, 2006.
36. †*Li,
Y., and Goodwin D. C. “Central participation of an interhelical insertion in
catalase-peroxidase bifunctionality and resistance to peroxide-dependent
inactivation.” Southeast Regional Meeting
of the American Chemical Society, Research Triangle Park, NC, November 11,
2004.
35. †*Baker,
R. D., *Cook, C. O., and Goodwin D. C. “Essential contribution of the C-terminal
domain to the structure of the catalase-peroxidase active site.” Southeast
Regional Meeting of the American Chemical Society, Research Triangle Park, NC,
November 11, 2004.
34. †*Cook,
C. O., *Baker, R. D., and Goodwin, D. C. “Catalase-peroxidase active site
restructuring by a distant and inactive domain.” Southeast Regional Meeting of the American Chemical Society,
Research Triangle Park, NC, November 11, 2004.
33.
†**Laband,
K. A., *Baker, R. D., and Goodwin, D. C. “Contributions of an interdomain
ion pair to the bifunctional properties of catalase-peroxidases.” Southeast
Regional Meeting of the American Chemical Society, Research Triangle Park, NC,
November 13, 2004. (2nd Place
Award Undergraduate Talk, Inorganic Division).
32. *Varnado, C. L., and
Goodwin D. C. Heme- and peroxide-dependent formation of a novel crosslink in
catalase-peroxidases. Southeast Regional Meeting of the American
Chemical Society, Research Triangle Park, NC, November 10, 2004.
31. *Varnado, C. L., and Goodwin, D. C. “Characterization of a novel
periplasmic catalase-peroxidase. Southeast
Regional Meeting of the American Chemical Society, Atlanta, GA., November
17, 2003.
30. †*Baker, R., and Goodwin D. C. Insight into the Role of the
C-Terminal Domain in Catalase-Peroxidase Function. Southeast Regional Meeting of the American Chemical Society,
Atlanta, GA, November 17, 2003.
29. †**Laband, K. A., and Goodwin D. C.
“Peroxidase-catalyzed oxidation of plant-derived o-methoxyphenols: Implications for the metabolism of health-promoting
phenolic compounds.” Southeast Regional
Meeting of the American Chemical Society, Atlanta, GA, November 18, 2003. (1st Place Award Undergraduate
Poster)
28. †*Li, Y., and Goodwin D. C. “Use of deletion mutagenesis to determine
the novel functions of two unique interhelical insertions in catalase-peroxidases.
Southeast Regional Meeting of the
American Chemical Society, Atlanta, GA, November 18, 2003.
26. †*Baker, R., and Goodwin, D. C. “Essential role of the C-terminal domain in catalase-peroxidase function.” American Chemical Society, 226th National Meeting, New York, NY, September 9, 2003.
25. †*Li, Y., and Goodwin, D. C. “Roles of two interhelical insertions in catalase-peroxidase bifunctionality.” American Chemical Society, 226th National Meeting, New York, NY, September 9, 2003.
24. †*Varnado, C. L., **Hertwig, K. M., **Thomas, R., **Roberts, J. K., and Goodwin, D. C. 2003. “Spectral and kinetic properties of a novel periplasmic catalase-peroxidase.” American Chemical Society, 226th National Meeting, New York, NY, September 10, 2003.
23. †*Goodwin, D. C., *Baker, R., *Varnado, C. L., and *Li, Y. “Protein
structural contributions to the unique catalytic properties of catalase-peroxidases.
Gordon Conference: Enzymes, Coenzymes,
and Metabolic Pathways, Meriden, NH, July 14-17, 2003.
22. †*Varnado, C. L., and Goodwin, D. C. “Design of a
specialized expression system for recombinant hemoproteins.” Southeast Regional Meeting of the American
Chemical Society, Charleston, South Carolina, November 14, 2002.
21. †*Baker, R., *Li, Y., and Goodwin D. 2002. Selective elimination
of catalase activity from catalase-peroxidase by deletion mutagenesis. Southeast Regional Meeting of the American
Chemical Society, Charleston, South Carolina, November 15, 2002.
20. †Goodwin, D. C., *Li, Y., and *Baker, R. Selective elimination
of catalase activity from catalase-peroxidase by deletion mutagenesis. Gordon Conference: Enzymes, Coenzymes, and
Metabolic Pathways, Meriden, NH, July 23 - 24, 2002.
19. †**Hertwig, K. M., and Goodwin, D.
C. “Characterization of a novel, extracellular catalase-peroxidase from E. coli O157:H7.” Council on Undergraduate Research, Posters on the Hill Forum,
Washington, D.C. April 18, 2002.
18. †**Hertwig, K. M. and Goodwin, D.
C. “Cloning, overexpression,
purification, and characterization of catalase/peroxidase from
enterohemorrhagic E. coli O157:H7.” Amer. Chem. Soc. Southeast Regional Meeting,
Savannah, GA, September 25, 2001
17. †*Li, Y., Melius, P., and Goodwin, D. C. “Activation of bacterial
catalase-peroxidases by addition of hemin.” Amer.
Chem. Soc., Southeast Regional Meeting, Savannah, GA, September 24, 2001.
16. †*Hertwig, K. and Goodwin, D. C. Cloning,
overexpression, purification, and characterization of catalase/peroxidase from
enterohemorrhagic E. coli O157:H7. Amer. Chem. Soc. 222nd National Meeting,
Chicago, IL, August 28, 2001.
Resulting from research before
coming to Auburn University
15. †Goodwin, D.C., Rowlinson, S. W.,
and Marnett, L. J. 1998. Heme oxidation states in prostaglandin
endoperoxide H synthase catalytic mechanism. Amer. Chem. Soc. 216th National Meeting, Boston, MA.
14. †Rowlinson, S.W., Crews, B. C., Goodwin D. C., and Marnett L. J. 1998. Structure/function analysis on the
cyclooxygenase channel of mouse prostaglandin endoperoxide synthase-2.
Amer. Chem. Soc. 216th National Meeting,
Boston, MA.
13. †Goodwin, D.C., Gunther, M. R., Hsi,
L. C., Crews, B. C., Eling, T. E., Mason, R. P., and Marnett, L. J. 1997. Nitric oxide trapping of the Y385
radical during prostaglandin endoperoxide synthase turnover. Intl. Congress Biochemistry Mol. Biol./Amer.
Soc. Biochemistry Mol. Biol. Joint Meeting, San Francisco, CA.
12. †Goodwin, D.C., Aust, S. D., and Grover, T. A. 1996.
Enhancement of peroxidase-catalyzed oxidation of hydrazine derivatives
by chlorpromazine. Amer. Soc.
Biochemistry Mol. Biol. National Meeting, New Orleans, LA.
11. †Goodwin, D.C., Aust, S. D., and Grover, T. A. 1996.
Enhancement of peroxidase-catalyzed xenobiotic oxidation by
phenothiazines. Soc. Toxicol.
Annual Meeting, Anahiem, CA.
10. †Goodwin, D.C., Aust, S. D., and Grover, T. A. 1995.
Phenothiazines as redox mediators in peroxidase-catalyzed xenobiotic
oxidation. Soc. Toxicol.
Mountain West Chapter Annual Meeting, Ft. Collins, CO.
9. †Goodwin, D. C., Yamazaki, I., Aust, S. D., and Grover, T.
A. 1995.
Determination of transient-state rate constants for peroxidase
reactions. Amer. Soc. Biochemistry Mol.
Biol./Amer. Chem. Soc. Div. Biol. Chem. National Meeting, San Francisco,
CA.
8. †Goodwin, D.C., Aust,
S. D., and Grover, T. A. 1995. Redox mediators in lignin peroxidase
catalysis: A kinetic model. Amer. Soc.
Biochemistry Mol. Biol./Amer. Chem. Soc. Div. Biol. Chem. National Meeting, San
Francisco, CA.
7. †Grover, T.A.,
Goodwin, D. C., Barr, D. P., and S.D. Aust.
1994. Protection of lignin
peroxidase activity: oxalate and cation radicals. Intl. Soc. Free Rad. Res. 7th Biennial Meeting, Sydney,
Australia.
6. †Goodwin, D.C., Aust,
S. D., and Grover, T. A. 1994. Veratryl alcohol (VA)
mediated oxidation by lignin peroxidase.
Intl. Soc. Free Rad. Res. 7th Biennial Meeting, Sydney, Australia.
5. †Goodwin, D.C., Barr,
D. P., Aust, S. D., and Grover, T. A. 1994. Inactivation of lignin peroxidase
of Phanerochaete chrysosporium by
oxygen radicals. Amer. Soc. for
Microbiol. 94th General Meeting, Las Vegas, NV.
4. †Goodwin, D. C.,
Barr, D. P., Aust, S. D., and Grover, T. A. 1994. The novel role of the fungal
metabolite oxalate in the catalytic cycle of lignin peroxidase. Amer. Soc. Microbiol. Intermountain Branch Annual Meeting,
Provo, UT.
3. †Goodwin, D. C., Johnston, C. G., Aust, S. D., and Grover,
T. A. 1993. Microwave extraction of DNA from fungi in soil: a simple, rapid
method for polymerase chain reaction. Amer.
Soc. Microbiol., 93rd General Meeting, Atlanta, GA.
2. †Johnston, C.G.,
Goodwin, D. C., and Aust, S. D. 1994. Use of ribosomal DNA for species
delineation and detection of Phanerochaete spp. Amer. Soc. Microbiol. 94th General
Meeting, Las Vegas, NV.
1.
†Goodwin, D.C., and Lee, S. B. 1992. Ribosomal DNA sequences
of Leptomitus lacteus, Sapromyces elongatus, Aquilinderella fermentans,
and Rhipidium sp. and their evolutionary implications for
the Oomycete order Leptomitales. Soc. Study Evol., University of
California, Berkeley, CA.
4.B.c.4. Auburn University Publications and Presentations:
(† denotes
the presenter, oral if underlined; * denotes graduate student coauthor; **
denotes undergraduate coauthor)
22. †**Warner, D., *Alam, M. J., *Moen,
F., Noel, Z., Goodwin, D. C., and Liles, M. “Identifcation
of Bacillus strains that inhibit
plant fungal and/or oomycete pathogens.” 2020 Auburn Research: Virtual Student Symposium, March 2021.
21. †**Forbes, M. G., **Minton, L. E., *Krewall,
J. R., and Goodwin, D. C. “Identifying heme intermediates of protein-based
cofactor formation in catalase-peroxidase (KatG).” 2020 COSAM Undergraduate Research Fair,
November 2020.
20. †**Minton, L. E.,
*Krewall, J. R., *Xu, H., and Goodwin, D. C. “The
effect of a pH-dependent arginine switch on protein-based cofactor formation in
catalase-peroxidase (KatG).” 2020 Auburn Research: Virtual Student Symposium, April 2020. (UG
Poster Award Winner for COSAM)
19. †**Sahrman, P., **McWhorter, K., *Krewall,
J. R., and Goodwin, D.C. 2018. “Electron-hole hopping as catalytic self-preservation: How
catalase-peroxidase from Mycobacterium tuberculosis avoids the perils of
peroxide decomposition.” Auburn U.
J. Undergrad. Scholarship (AUJUS) 7,
47 – 48.
18. †**McWhorter, K. “Exploiting active-site tryptophans for off-pathway electron transfer: Preserving the activity of peroxide detoxifying enzymes.” This is Research Student Symposium, March 26, 2018.
17. †**Sahrmann, P. “Electron-hole hopping as catalytic
self-preservation: How catalase-peroxidase from M. tuberculosis avoids the perils of peroxide decomposition.” This is Research, Student Symposium,
March 26, 2018.
16. †*Njuma,
O.J. “Radical Mechanisms for Catalase-Peroxidase (KatG) activity, inactivation, and restoration” This is Research, Student Symposium, April
13, 2016.
15. †**Snider, O.H. “Kanamycin oxidation by KatG: A new mechanism for aminoglycoside anitibiotic resistance?” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 24, 2015.
14. **McCurdy, E., **Barr, L.E., *Njuma, O.J., *Ndontsa, E.N., and Goodwin, D.C. 2015. Evaluating the novel role of Trp 438 in active turnover of M. tuberculosis catalase-peroxidase. Auburn U. J. Undergrad. Scholarship (AUJUS) 4, 27 – 32.
13. †**Kollhoff, A., and Goodwin, D.C. “Production of a tuberculosis shikimate kinase variant for inhibitor analysis by mechanistically targeted intrinsic protein fluorescence” This is Research, Student Symposium, April 13, 2015.
12. †*Njuma, O.J. “Potential participation of the proximal tryptophan and arginine switch in catalase-peroxidase inactivation.” This is Research, Student Symposium, April 13, 2015.
11. †**Barr, L.E, **McCurdy, E., *Njuma, O., and Goodwin, D.C. “Evaluating potential routes of off-pathway electron transfer in catalase-peroxidases.” This is Research, Student Symposium, April 13, 2015.
10. †*Fuanta, N.R. “Site-directed incorporation of intrinsic fluorescence in shikimate kinase to evaluate catalysis and inhibition.” This is Research, Student Symposium, April 13, 2015.
9. †**Kollhoff, A., and Goodwin, D.C. “Production of a tuberculosis shikimate kinase variant for inhibitor analysis by mechanistically targeted intrinsic protein fluorescence” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 25, 2014.
8. †**Gill, G., and Goodwin, D.C. “Isolation and kinetic characterization of Mycobacterium tuberculosis shikimate kinase.” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 26, 2013.
7. †Goodwin, D.C. “Novel mechanisms for hydrogen peroxide degradation catalyzed by KatG: Implications for antibiotic resistance and bacterial virulence.” Pharmacal Sciences Graduate Seminar, April 10, 2012.
6. †**Suh, Jordan, and Goodwin, D.C. “Using cysteine substitutions to investigate unique structural features of KatG.” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 26, 2011.
5. †**Ransom, S. “The integral roles of peripheral protein structures in the function of KatG from Mycobacterium tuberculosis.” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 28, 2010.
4. †Goodwin, D.C. “A tale of two domains: How long-distance relationships modulate enzyme function.” Special Topics in Kinesiology, B. Gladden (faculty organizer), School of Kinesiology, October 1, 2009.
3. †**Campbell, R. “Contribution of an interhelical insertion to catalase-peroxidase bifunctionality and resistance to peroxide-dependent inactivation.” AU Undergraduate Research Forum, March 13, 2009.
2. †**Campbell, R. “Contribution of an interhelical insertion to catalase-peroxidase bifunctionality and resistance to peroxide-dependent inactivation. AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, August 8, 2008.
1. †**Hertwig, K. “Cloning, overexpression, purification, and characterization of catalase/peroxidase from enterohemorrhagic E. coli O157:H7.” Auburn University Graduate Research Forum, Auburn, AL. 2001.
4.B.f. Patents
and Inventions
3. Hong, J. W., Goodwin, D., Duin, E. C., Jambovane, S., *Moore, R., Nam, T.-J., and Kim, S.-K. Systems for and methods of characterizing reactions. U.S. Patent Application # 2010/0311,611.
2. *Varnado, C., Olson, J. S., and Goodwin, D. C. Increasing recombinant Hemoglobin expression for blood substitute production in E. coli by Co-Expression with the heme receptor gene (chuA) from E. coli 0157:H7. Invention Disclosure Filed with Rice University.
1. Goodwin, D. C., and *Varnado, C. System for the Expression of Recombinant Hemoproteins in Escherichia coli. U.S. Provisional Patent # 60/375,347
4.B.g. Grants and Contracts
4.B.g.1. Extramural Sources
Submitted:
Current
Funding:
Previously Funded:
National Science Foundation (MCB-1616059)
PI: Goodwin, D. C.
Dates: 8/1/16 – 7/31/21
Title: Conduits and Control of KatG Intramolecular Electron Transfer: Formation and Operation of a Novel Cofactor
Amount: $569,549
National
Institutes of Health (2R01DK093810-04)
PI: Easley, C.J.
Co-PI: Judd, R.; Co-I: Goodwin, D.C.
Dates: 02/17/16 – 02/28/17
Title: Mouse-on-a-chip systems to evaluate pancreas-adipose tissue dynamics in vitro
Amount: $1,463,980
Contribution: 5%; my role on this project is related to my background in nutritional biochemistry.
National Science Foundation (MCB-0641614)
PI: Goodwin, D. C.
Dates: 7/1/07 – 6/30/12
Title: Indispensable roles of an inactive domain in catalase-peroxidase catalysis: Applications for enzyme engineering
Amount: $434,182
National
Science Foundation (MCB-0641614 - supplement)
PI: Goodwin, D. C.
Dates: 7/1/09 – 6/30/10
Title: Indispensable roles of an inactive domain in catalase-peroxidase catalysis: Applications for enzyme engineering (Supplement)
Amount: $25,353 (for upgrade of Applied Photophysics Stopped-Flow spectrometer)
USDA, Hatch Grant and Alabama Agricultural Expt Station Special Grants Program PD: Whitley, E.
Co-PDs: Wolfe, D., Edmonson, M., Goodwin, D.C.
Dates: 6/01/07 – 5/31/08
Title: Development of Vaccines Targeting Horn Flies
Amount: $185,000
Contribution: 5%; a minimum of summer salary support; one laboratory undergraduate contributed to the project
USDA
CSREES (2006-34528-17542)
PD: Wolfe, D. F.
Co-PD’s: Whitley, E., Abrams, M., Zhang, D., Goodwin, D. C.
Dates: 05/15/06 – 05/14/07
Title: Immunization of cattle against horn fly blood feeding
Amount: $185,000
Contribution: 5%; a minimum of summer salary support; one laboratory undergraduate contributed to the project
Petroleum Research Fund, American Chemical Society (38802 – G4)
PI: Goodwin, D. C.
Dates: 01/01/03 – 09/31/05
Title: Understanding the bifunctional active site of catalase-peroxidases: Insights for enzyme engineering.
Amount: $35,000.
Not funded:
National Science Foundation (STTR NSF 2208111)
PI: Mead, D. (Terra Bioworks, Inc.)
Co-PIs: Noel, Z. A., Liles, M. R., and Goodwin D. C.
Title: STTR Phase I: Synthetic biology solutions for microbial crop protection against fungal and oomycete pathogens
Amount: $257,117
National Science Foundation
PI: Ellis, H. R.
Co-PIs: Goodwin, D. C., Suh, S.-J., Hamid, A.,
Dates: 6/01/20 - 5/31/22
Mapping the Metabolic Impact of Sulfur Limitation on the Terrestrial Microbiome
Amount: $435,212.14
Contribution: Effort 15%; Funds ~15% Drs. Ellis and Goodwin co-advise a graduate whose support is proposed in this application.
(Submission Deadline: March 2, 2020)
National Institutes of Health (NIAID R15 AI147315-01)
PI: Goodwin, D.C.
Co-I: Calderón, A.
Dates: 6/01/19 - 5/31/21
Strategies to identify and assess chemical probes against mycobacterial shikimate kinase: From mechanisms of inhibition to metabolomics.
Amount: $437,404
National Institutes of Health (NAID R15 AI113684-01A1)
PI’s: Calderón, A.I., Goodwin, D. C.
Submitted: 10/25/17
Title: Strategies for uncovering selective and mechanistically appropriate natural product inhibitors of Mycobacterium tuberculosis shikimate kinase.
Amount: $438,313
Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)
National Institutes of Health (NAID R15 AI113684-01A1)
PI’s: Calderón, A.I., Goodwin, D. C.
Submitted: 06/25/15
Title: Toward New Antitubercular Drugs: Uncovering Mechanistically Appropriate Inhibitors of Mycobacterium tuberculosis Shikimate Kinase from Natural Products
Amount: $437,931
Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)
National Science Foundation (MCB 1517433)
PI: Goodwin, D. C.
Submitted: 11/17/14
Title: Maximizing Cellular Resistance to Hydrogen Peroxide: Synergy Between KatG Activities
Amount: $523,259
National Science Foundation (MRI 1429654)
PI: Mansoorabadi, S.
Co-PI’s: Duin, E.C., Ellis, H.R.
Role: Contributed to the proposal as a major user/collaborator
Submitted: 01/23/14
Title: Acquisition of a Rigaku Protein Structure Workbench
Amount: $694,756
National Institutes of Health (NIAID R15 AI113684)
PI’s: Calderón, A.I., Goodwin, D.C.
Submitted: 10/25/13
Title: Toward New Antitubercular Drugs: Uncovering Mechanistically Appropriate Inhibitors of Mycobacterium tuberculosis Shikimate Kinase from Natural Products
Amount: $444,000
Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)
National Science Foundation (CLP 1306931)
PI: Goodwin, D. C.
Submitted: 10/31/12
Title: Synergy Not Antagonism in Antioxidant Defenses: How Peroxidatic Electron Donors Make KatG a Novel and More Efficient Catalase
Amount: $539,972
National Science Foundation (CLP 1214099)
PI: Goodwin, D. C.
Submitted: 11/30/11
Title: Enlisting Peroxidatic Electron Donors to Exapand the Catalytic Activity of KatG: Implications for the Baterial Response to Hydrogen Peroxide
Amount: $525,555
National Science Foundation (DUE 0728674)
PI: Marcy, R.
Co-PI’s: Newton, S., Armstrong, A., Long, V., Goodwin D. C.
Submitted: 02/16/07
Title: ASCC: Adaptive, Science, Customization, Curriculum
Amount: $597,243
National Science Foundation (DBI 0649881)
PI: Hong, J.W.
Co-PI: Goodwin D. C.
Submitted: 08/25/06
Title: Development of a Novel Protein Kinetics Landscaper for Biological Catalysis
Amount: $383,720
Contribution: 25%
National Science Foundation (MCB 0516905)
PI: Goodwin, D. C.
Submitted: 01/12/05
Title: Vital Roles of an “Inactive” Domain in Catalase-peroxidase Catalysis
Amount: $398,308
National Science Foundation (MRI 0521180)
PI: Shannon, C.
Co-PI’s: Cheng, Z., Prorok, B., Goodwin D. C., Park, M.
Submitted: 01/27/05
Title: A Raman Spectroscopy User Facility at Auburn University
Amount: $445,000
National Institutes of Health (R01 GM069638-01A1)
PI: Goodwin, D.C.
Submitted: 03/01/04
Title: Vital Role of an Inactive Domain in Catalase-Peroxidases
Amount: $572,242
Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)
National Science Foundation (MCB 0417109)
PI: Goodwin, D. C.
Submitted: 01/12/04
Title: Vital Roles of an “Inactive” Domain in Catalase-peroxidase Catalysis
Amount: $369,168
National Institutes of Health (R01 GM069638-01)
PI: Goodwin, D.C.
Submitted: 02/01/03
Title: Vital Role of an Inactive Domain in Catalase-Peroxidases
Amount: $572,242
National Science Foundation (MCB 0315894)
PI: Goodwin, D. C.
Submitted: 01/10/03
Title: Vital Roles of an Inactive Domain in Catalase-peroxidase Catalysis
Amount: $285,089
National Institutes of Health (R15 DK60500)
PI: Goodwin, D. C.
Submitted: 01/17/10
Title: ONOO- Reduction by E. coli O157:H7 Catalase-Peroxidase
Amount: $143,000
National Science Foundation (MRI 0078857)
PI: Albrecht-Schmitt, T.A.
Co-PI’s: Goodwin, D.C., Cammarata, V., Schevlin, P., Stanbury, D.M.
Submitted: 01/13/00
Title: Acquisition of a single crystal X-ray diffractometer for structural studies on new materials, small molecules and biomolecules
Amount: $203,490
4.B.g.2. Internal Sources
Intramural
Grants Program
PI: Calderón, A.
Co-PI: Goodwin, D.C.
Dates: 3/1/13 – 2/28/15
Title: Toward new antitubercular drugs: Uncovering mechanistically appropriate inhibitors of Mycobacterium tuberculosis shikimate kinase from natural products
Amount: $54,000
Promoting Research in Sciences and Mathematics (PRISM), COSAM
PI: Goodwin, D. C.
Co-PI’s: Ellis, H.R., Singh, N., Duin, E.
Dates: 03/20/04 – 03/19/05
Title: Circular dichroism at Auburn University (Externally Reviewed)
Amount: $100,000
Auburn
University Biogrants Program
PI: Goodwin, D. C.
Dates: 05/01/01 – 09/30/03
Title: Mechanisms of heme acquisition by enterohemorrhagic E. coli strain O157:H7 (Externally Reviewed)
Amount: $20,323
Dean’s Research Initiative Grant, COSAM
PI: Goodwin, D. C.
Dates: 11/01/00 – 10/31/01
Title: Mechanisms of heme acquisition by pathogenic bacteria.
Amount: $10,000.
Competitive Research Grant, Office of the Vice President for Research
PI: Goodwin, D. C.
Dates: 05/01/00 – 04/30/01
Title: Function of catalase-peroxidase from Enterohemorrhagic Escherichia coli O157:H7.
Amount: $10,000
Small Equipment Grant, Office of the Vice President for Research
PI: Goodwin, D.C.
Dates: 10/01/99 – 09/30/00
Title: Proposal for the Purchase of an Ultralow Freezer for the Storage of Temperature Sensitive Biochemical Research Materials
Amount:
$4,797
New Faculty Start-Up, Department of Chemistry/COSAM/OVPR
PI: Goodwin, D.C.
Dates: 10/01/99 – 09/30/02
Amount: $160,000
4.B.g.3. Other
Dr. G. Lynn and Cheryl Marks Family Scholarship for Undergraduate
Research
A donation from the Marks family and matched by GlaxoSmithKline was established and earmarked specifically to support an undergraduate student each year working on M. tuberculosis related proteins in my laboratory. The scholarship pays a stipend to the student of $2000 for the year.
4. C. OUTREACH |
4.C.a.
Commentary
Prison Education Outreach
With nearly 570 prisoners per 100,000 residents, Alabama has the ninth highest incarceration rate in the United States, a statistic made more alarming by the fact that the United States has the highest incarceration rate in the world. There are nearly 28,000 prisoners in the Alabama Department of Corrections (ADOC) system.1 At the same time, opportunities for prisoners to better themselves through education remain extremely limited. Despite the well-documented benefits of educational programs for prisoners, their families, and their communities, only about 2% of the ADOC prison population is involved in educational programming of any kind. Having successfully implemented several arts and humanities courses, the Alabama Prison Arts + Education Project (APA+EP) sought to address the pressing need for and very strong interest of prison-based students in STEM education opportunities. The SPARKs in Science and Mathematics lecture series was one avenue by which the APA+EP sought to pursue this objective. SPARKs is a seminar series presented by Auburn University faculty from the Colleges of Sciences and Mathematics, Agriculture, and Engineering. Participating faculty each present a single lecture on the area of their expertise in an ADOC facility. Over a 10 – 12 week series, a broad and engaging set of topics are vigorously engaged by the students, serving to pique the interest of students in pursuing additional education in the STEM courses that the APA+EP continues to develop.
I gave my first SPARKs series talk in Spring 2012, and I was won over by a great group of highly engaged students. I received so many questions from the students that an hour of
prepared material took the full two-hour seminar period to cover. That experience changed my life. I was won over by the enthusiasm and engagement of the students so much so that I then not only participated in SPARKs every year, but I sought to recruit as many of my colleagues to participate as possible.
1Hinds, O. et al. People in Prison 2017. Vera
Institute of Justice, https://www.vera.org/publications/people-in-prison-2017 |
|
The impact of the SPARKs emanates in multiple directions to the benefit of APA+EP students and teachers, alike. First, the students have the opportunity to engage discussions in STEM topics that they might not encounter otherwise. As one of our students has said, “These [lectures] are more exciting because they all take me to places I’ve never thought of.” As importantly, material presented in the prison classroom never remains contained within that space. Rather, the material is discussed and shared with others who were not in attendance, contributing positively to the education (formal and informal) of others. With respect to an impact on other formal educational programs, one of our students has reported, “I teach pre-GED on Tuesdays and Thursdays and will share some of the General Education materials with the students.” Likewise, by less formal (but no less important) mechanisms, another of our students has written, “These classes have become well known in the camp and the younger men are becoming interested and that’s a good thing, getting them to think in another direction. Those that attend find that they have constructive conversations rather than those of the convict mentality.”
Participation in SPARKs has had a profound impact on me and my teaching, and as a result, has been a benefit to the Auburn University students who come through my courses. First, participation in APA+EP has changed the way I think about prisons, criminal justice reform, and most of all, the many APA+EP students seeking to better themselves through education. Second, teaching in prison-based ‘classrooms’ has done more to spur innovation and creativity in my own teaching than anything else I have done. Although technology can enable teachers to engage students in ways not possible even a few years ago, it is important to recognize that the use of technology is not necessarily the same thing as innovation. Indeed, it is precisely the limitations imposed by the prison ‘classroom’ that have produced some of the most notable changes to my teaching in the university setting. For example, there is no internet access, and it is a felony to carry a cell phone into a prison. In addition, one is confronted with a greatly varied audience in terms of background in the subject. One must find ways to effectively bring the material across to an audience where some of the students present may never have finished sixth grade and others may have Master’s degrees and/or some professional school training. My experiences in SPARKs have made me a better communicator of challenging concepts in my university classrooms. The Molecular Players Theater where I enlist the assistance of students to help me physically act out complex mechanisms was developed in large part through my SPARKs presentations. It is about as low-tech as one could possibly get. For example, the classroom space comes to represent the separation between active sites in the pyruvate dehydrogenase complex, student ‘volunteers’ become cofactors as identified by the paper placards they carry, steps like decarboxylation are manipulations (e.g., literally tearing) of paper representations of substrates, and the channeling of intermediates from one active site to the next has me running from one end of the classroom to the other. By way of the feedback I receive from them in formal teaching evaluations and in informal conversation, these are the kinds of things that my Auburn University students remember most about their time in my courses.
Finally, it is important to mention that innovations also carry the other way (i.e., Auburn to prison classroom), albeit at a slower, security-limited pace. In my most recent SPARKs presentation, I was able to take materials into the facility to carry out various aspects of the peroxidase demonstration for the students. In this way, SPARKs model is one that may be particularly effective in enabling expansion of what is allowed in the prison classroom. By individual faculty presenters going through what is necessary to try a new approach in a
single lecture, prison administration is able to observe, on a small scale, that the activity in question can be carried out while minimizing risks to security. The expectation is that these small steps will pave the way for future prison classroom innovations.
Summer Bridge: Building Awareness of and Engagement
in Undergraduate Research
The Summer Bridge Program is designed to assist
incoming COSAM freshmen who are from groups underrepresented in STEM careers to
make the transition to the collegiate environment. It is a Summer
mini-mester of courses that provides foundational
content that facilitates success in navigating the challenging courses of COSAM
curricula. The program also teaches effective study habits and time-management
skills to help increase success in undergraduate study, ultimately leading to graduation.
Data are showing that undergraduate research
experiences provide a myriad of benefits to the students who participate.2
I have come to the same conclusions by observing the undergraduates who have
worked in my laboratory. Participation in undergraduate research, then,
represents a powerful instrument that aligns well with the objectives of the
Summer Bridge program. Together, my colleague, Dr. Holly Ellis, and I developed
a two-part contribution to the Summer Bridge program designed to increase
awareness of and participation in undergraduate research.
Research Q
and A. The purpose of this
session/lecture is to encourage participation of these incoming undergraduates
in research programs as their academic programs progress. It is anticipated
that promotion of research activities to Summer Bridge participants as they
enter the university will lead to their application for fellowships later in
their undergraduate programs.
Hands
on undergraduate research demonstration. Students participate in a redox biochemistry experiment
based on peroxidase chemistry. The results are visually colorful/striking. The
exercise is a fun way to get pipettors in hand, propose and perform a short
experiment, and evaluate the results. Importantly, among the materials used are
modified enzymes originally produced by undergraduate researchers in the
Goodwin Laboratory (e.g., Robert Campbell’s KatG[D209-228]).3
Applications of the Peroxidase Demonstration
As mentioned above and illustrated in previous sections (4.A.g Other Contributions to Teaching), the peroxidase system is highly adaptable to a wide range of educational applications. It can be used as a front-of-classroom demonstration of multiple chemical/biochemical concepts (e.g., enzyme catalysis, redox titration, free-radical chemistry, anti-oxidant properties of foods and vitamins, etc.). Similarly, in outreach activities like Summer Bridge, this system is adaptable to hands-on activities of varying depth and complexity, depending on the time available and the goals of a given program. An added attractive feature of this system is its versatility in terms of the materials that can be used and the relatively low cost of purchasing them. As such, I have adapted this system for use by students in Science Olympiad or Teaching Enhancement Award activities, and even at home with commonly available materials.
2Lopatto, D. Undergraduate Research as a High-Impact
Student Experience. 2010. Peer Review
12. AACU 3Kudalkar, S.N., et al. J. Inorg. Biochem.
116, 106 – 115. |
4.C.b.
Activities and Products
4.C.b.1.
Instructional Activities
Prison-based education: SPARKs in Science and Mathematics
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
Proteins, radicals, vitamins, and minerals: How biology makes metabolism
work.
Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in
Audience: APA+EP students of Tutwiler Correctional Facility,
Wetumpka, AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 03/30/22
Role: Material/Demonstration Developer
and Presenter
Organizing faculty presenters for prison
lecture series
Title:
SPARKS in Science and Mathematics
Duration: 20 hours soliciting presenters
and preparing presentation schedule
Audience: APA+EP students of Tutwiler Correctional Facility,
Wetumpka, AL.
Method: e-mail communication
Dates: 10/01/21 – 01/30/22 (Initial
e-mail thru faculty presenter security training)
Role: Faculty organizer
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
Proteins, radicals, vitamins, and minerals: How biology makes metabolism
work.
Duration: 2 hours classroom time; 2.5
hours drive time; 1 hour security check-in
Audience: APA+EP students of Ventress Correctional Facility, Clayton, AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 03/06/19
Role: Material/Demonstration Developer
and Presenter
Organizing faculty presenters for prison
lecture series
Title:
SPARKS in Science and Mathematics
Duration: 20 hours soliciting presenters
and preparing presentation schedule
Audience: APA+EP students of Ventress Correctional Facility, Clayton, AL.
Method: e-mail communication
Dates: 10/01/18 – 01/30/19 (Initial
e-mail thru faculty presenter security training)
Role: Faculty organizer
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
Proteins, radicals, vitamins, and minerals: How biology makes metabolism
work.
Duration: 2 hours classroom time; 2.5
hours drive time; 1 hour security check-in
Audience: APA+EP students of Staton Correctional Facility, Elmore, AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 04/20/18
Role: Material/Demonstration Developer
and Presenter
Organizing faculty presenters for prison
lecture series
Title:
SPARKS in Science and Mathematics
Duration: 20 hours soliciting presenters
and preparing presentation schedule
Audience: APA+EP students of Staton Correctional Facility, Elmore, AL.
Method: e-mail communication
Dates: 09/15/17 – 01/26/18 (Initial
e-mail thru faculty presenter security training)
Role: Faculty organizer
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
How cells make molecules that work: Sensors, pumps, motors, and power generators.
Duration: 2 hours classroom time; 2.5
hours drive time; 1 hour security check-in
Audience: APA+EP students of Tutwiler Correctional Facility,
Wetumpka, AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 03/13/17
Role: Material/Demonstration Developer
and Presenter
Organizing faculty presenters for prison
lecture series
Title:
SPARKS in Science and Mathematics
Duration: 20 hours soliciting presenters
and preparing presentation schedule
Audience: APA+EP students of Tutwiler Correctional Facility, Elmore,
AL.
Method: e-mail communication
Dates: 11/4/16 – 02/06/17 (Initial e-mail
thru faculty presenter security training)
Role: Faculty organizer
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
How cells make molecules that work: Sensors, pumps, motors, and power
generators
Duration: 2 hours classroom time; 3.5
hours drive time; 1 hour security check-in
Audience: APA+EP students of Easterling Correctional Facility, Clio,
AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 03/28/16
Role: Material/Demonstration Developer
and Presenter
Organizing faculty presenters for prison
lecture series
Title:
SPARKS in Science and Mathematics
Duration: 20 hours soliciting presenters
and preparing presentation schedule
Audience: APA+EP students of Easterling Correctional Facility, Clio,
AL.
Dates: 11/01/15 – 02/12/16 (Initial
e-mail thru faculty presenter security training)
Role: Faculty organizer
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
Protein structure and function: Building and managing catalysts for life
Duration: 2 hours classroom time; 2.5 hours
drive time; 1 hour security check-in
Audience: APA+EP students of Staton Correctional Facility, Elmore, AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 02/26/15
Role: Material/Demonstration Developer
and Presenter
Organizing faculty presenters for prison
lecture series
Title:
SPARKS in Science and Mathematics
Duration: 20 hours soliciting presenters
and preparing presentation schedule
Audience: APA+EP students of Staton Correctional Facility, Clio, AL.
Method: e-mail communication
Dates: 11/04/14 – 02/04/15 (Initial
e-mail thru faculty presenter security training)
Role: Faculty organizer
Special Grant Program in Chemical
Sciences (preproposal)
The Camille and Henry Dreyfus Foundation,
Inc.
PI: Goodwin, D.C.
Co-PI: Shannon, C.
Title: Expanding educational opportunity
through chemistry
Duration: 09/01/14 – 08/31/15
Amount: $27,400
Description: The project was to establish
a chemistry course for an ADOC facility drawing on departmental faculty
teaching expertise course and a general science course for Alabama Prisoners
using iPads as a foundational teaching tool. In addition, the grant was to
support a SPARKs lecture series, and establish the SPARKs II-type lecture
series.
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Title:
Protein structure and function: Building and managing catalysts for life
Duration: 2 hours classroom time; 2.5
hours drive time; 1 hour security check-in
Audience: APA+EP students of Elmore Correctional Facility, Elmore,
AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: 02/13/14
Role: Material/Demonstration Developer
and Presenter
Guide for new prison lecture faculty
Title:
SPARKS in Science and Mathematics
Duration: 2 hours classroom time; 2.5
hours drive time; 1 hour security check-in for each of three presentations
Audience: APA+EP students of Elmore Correctional Facility, Elmore,
AL.
Method: Accompanied three new faculty
presenters to assist with security check-in, etc.
Dates: March 6 (C. Bailey, presenter),
April 3 (J. Feminella and B. Helms, presenters), and
April 10, 2014 (S. Rodning, presenter)
SPARKS in Science and Mathematics II, Faculty Prison Lecture Miniseries
Seminar Title: Building biology from the ground up: Atoms to molecular pumps and
power generators (3-part series)
Duration: 2 hours classroom time; 3.5
hours drive time; 1 hour security check-in for each of three trips; 7 hours
PREA and security training (01/07/14)
Audience: APA+EP students of Easterling Correctional Facility, Clio,
AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Dates: February 12, 19, and 26, 2014
Role: Material/Demonstration Developer
and Presenter
Auburn University Competitive Outreach
Grant
PI: Stevens, K., APA+EP Director
Co-PIs: Goodwin, D. C., and Wilson, A.
Title: Bridging the curriculum gap in
prisoner education: A collaboration of colleges
Duration: March 1, 2013 – February 28,
2014
Amount: $59,568
Description: The purpose of the grant was
to establish a mathematics course and a general science course for Alabama
Prisoners using iPads as a foundational teaching tool. In addition, the grant was
to support a SPARKs lecture series, and establish the SPARKs II-type lecture
series.
SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar
Seminar Title: Building Biology from the
Ground Up: Atoms to Molecular Pumps and Power Generators
Duration: 2 hours classroom time; 2.5
hours drive time; 1 hour security check-in
Audience: APA+EP students of Elmore Correctional Facility, Elmore,
AL.
Method: In-person site visit, lecture,
demonstration, and Q and A
Date: March 12, 2012
Role: Material/Demonstration Developer
and Presenter
Summer Bridge Program
Hands-on undergraduate research
demonstrations
Laboratory Title: Enzyme catalysis, free
radicals, and antioxidants
Duration: 2 hours presentation/laboratory
time; 12 hours preparation time (each date)
Audience: Students of the COSAM Summer
Bridge Program
Method: Laboratory technique
demonstration, scientific foundation/exposition, and experiment supervision
Dates: June 23, 2016; June 11, 2015; June
17, 2014; June 16, 2013; June 20, 2012.
Role: Primary organizer, lecturer, and
supervisor
Assistance: Typically, two graduate
students and two undergraduate students
Undergraduate research/research career
question and answer session
Session Title: Enhancing your
undergraduate education and experience through research
Duration: 1 hour presentation time; 2
hours preparation time (each date)
Audience: Students of the COSAM Summer
Bridge Program
Method: Co-led Q and A session with Dr.
Holly Ellis
Dates: June 6, 2017, June 10, 2015; June
13, 2014; June 15, 2013; June 13, 2012.
Role: Co-organizer and co-lecturer
Teaching Enhancement Award Activities
TEA 2009
Activities: High school student research
training (two weeks); High school teacher co-training (one week); closing
presentation preparation and delivery.
Project Title: Antioxidants: Totally rad!
Duration: Three 40-hour weeks
Participants: Kendall Hall (HS Student);
Lynn McCain (HS Teacher)
Dates: June 2009
Role: Identified, set up, and directed
the research project, trained the student in laboratory techniques, data
collection, and data analysis, advised on poster construction and final oral
presentation.
TEA 2007
Activities: High school student research
training (two weeks); High school teacher co-training (one week); closing
presentation preparation and delivery.
Project Title: Radical approach to
evaluating and teaching kinetics of antioxidants
Duration: Three 40-hour weeks
Participants: W.C. “Dub” Davison (HS
Student); Warren Hamm (HS Teacher)
Dates: June 2007
Role: Identified, set up, and directed
the research project, trained the student in laboratory techniques, data
collection, and data analysis, advised on poster construction and final oral
presentation.
Other Instructional Activities
Alabama Science and Engineering Fair
Activity: Best of Fair Judge; evaluated top candidates submitted by
Head Category Judges for Best of Fair awards, deliberated with other Best of
Fair Judges to down-select six finalists, panel review to select four
finalists.
Duration: 6 hours (day of event)
Dates: April 1, 2023
Science Olympiad
Activity: Represented the Department of Chemistry and Biochemistry,
assisting Mary Lou Ewald and Dr. Allen Lander (Chair, Department of Physics) in
the distribution of awards for Science Olympiad Events.
Duration: 2 hours (day of event)
Dates: March 26, 2022
Kitchen Biochemistry
Activity: Devised and implemented a set
of experiments in enzyme isolation and kinetic evaluation using materials
commonly available at the grocery store (horseradish root, hydrogen peroxide,
vinegar, liquid laundry detergent, etc.).
Duration: Three 1-hour in-laboratory
sessions; 4 hours communication/direction regarding the home/kitchen experience
Dates: Spring 2011
Role: Provided instruction to home school
students for performing experiments and making qualitative evaluations in their
own kitchens. Instructed students in the lab setting using advanced reagents
and instruments to do parallel experiments.
Middle School Science Olympiad
Duration: 10 hours (day of event); 30
hours preparation
Dates: February 28, 2009
Role: Chemistry section co-organizer
(with Dr. Holly Ellis); Co-Event
Supervisor (Experimental Design)
Middle School Science Olympiad
Duration: 5 hours (day of event); 20
hours preparation
Dates: March 2008
Role: Developed and implemented Food Science event
Community College Instructor Laboratory
Training
Participant: Dr. Ronald Marcy, Division
Chair, Biology and Chemistry, Alabama Southern Community College.
Duration: Several Saturdays over the
Spring semester of 2003.
Role: Supervised training for Dr. Marcy in
the Goodwin laboratory learning techniques, including site-directed
mutagenesis, recombinant protein expression, protein purification, and
enzymatic characterization. He then used this information to alter lecture and
laboratory courses at his home institution.
4.C.b.2. Technical Assistance
Destination STEM
Date: September 22, 2017
Participants: Rene Fuanta
and Dianna Forbes (Chemistry and Biochemistry graduate students) as
demonstrators for middle and HS students
Duration: 10 hours pre-event consultation
and instruction
Role: Trained and consulted with Rene and
Dianna on the set-up and execution of their peroxidase-based demonstration of
free radical chemistry.
4.3.b.5. Other Outreach Products
COSAM
Outreach in Prison
A seminar on the APA+EP to the COSAM Leadership Council
Date: October 2, 2015
Attendees: COSAM Leadership Council members and other stakeholders
Duration: 30 minutes
Role: Speaker
Promotional
video for the APA+EP
Dates: April 7, 2014 (interview shooting); November 2014 video review
Participants: Stevens, K., APA+EP Director
Beal, A., and Goodwin, D.C., APA+EP instructors
Duration: 4 hours total for interview and editorial review
Role: Interviewee
Link: Final video product (published December 1, 2014)
2014
AU Outreach Symposium (team presentation)
Title:
Bridging a Curriculum Gap in Prisoner
Education
Date: February 11, 2014
Participants: Stevens, K., APA+EP Director
Goodwin, D.C., Wilson, A., and Beal, A., APA+EP instructors
Duration: 1 hour presentation; 5 hours preparation
Role: Co-presenter
4.C.b.6. Outreach Grants
Auburn
University Competitive Outreach Grant
PI: Stevens, K.
Co-PIs: Goodwin, D.C.; Wilson, A.
Dates: 3/1/13 – 2/28/14
Title: Bridging the Curriculum Gap in Prisoner Education: A Collaboration of Colleges Innovating Solutions
Amount:
$59,568
4. D. SERVICE |
4.D.a. University Service (Current in Italics)
4.D.a.1. Department of Chemistry and Biochemistry Service:
Department Chair, Department of Chemistry and Biochemistry,
Auburn University, 07/20 – present.
Member, Chemistry and Biochemistry Leadership Council,
09/18 – present.
Member, COSAM Dean Search Committee (Department
Chairs’ representative) 08/21 – 04/22.
Member, COSAM Dean Search Committee (Department
Chairs’ representative) 11/20 – 04/21.
Presenter, Graduate Student Recruiting Invitational, Chemistry and Biochemistry, 11/08/19. Graduate School 101
Graduate Program Officer, 05/17 – 06/20.
Special Project, Graduate Handbook Major Revision, 01/20 – 06/20. Included implementation of committee-based annual reviews of graduate students, adoption of department-level Plan of Study procedures and protocols, enhanced mechanisms for committee selection, and institution of graduate student representatives.
Special Project, Graduate Handbook Major Revision, 02/18 – 10/18. Included substantial policy revisions, implementation of assessment procedures and instruments, soliciting DBC faculty and graduate student input, and obtaining faculty approval of individual components and the final Graduate Handbook.
Chair, Graduate Program Committee, 05/17 – 06/20.
Chair, Biochemistry Division, 05/05 – 05/19.
Developer, General Doctoral Exam (written and oral) assessment
rubrics
Manager, CD Spectropolarimeter, 06/04 – present.
Chair, Graduate Admissions Committee, 01/10 – 05/17.
Member, Graduate Recruiting/Visits/Admissions Committee, 08/06 – 12/09.
Member, Graduate Student Admissions Committee, 09/99 – 07/06.
Chair, Biological Instrumentation Committee, 08/06 – 05/09.
Manager, MALDI Mass Spectrometer, 09/04 – 05/09.
Member, Faculty Search Committee, Bioimaging and Biochemistry, 08/16 – 02/17. (Raj)
Chair, Biochemistry Faculty Search Committee, 08/11 – 05/12. (Mansoorabadi)
Member, Physical Chemistry Faculty Search Committee, 9/09 – 12/10.
(Patkowski)
Member, Departmental Faculty Council, 08/06 – 08/09.
Coordinator, Chemistry and Biochemistry Colloquium Program, 08/05 – 05/09.
Colloquium funding obtained:
Increasing the Caliber and Diversity of Chemistry and Biochemistry Colloquium COSAM; $37,500; 1/1/06 – 5/1/08.
Presenter, Faculty research synopses, ACS Auburn Section Student Affiliate, 02/19/09.
Presenter, Graduate Student Recruiting Invitational, Chemistry and Biochemistry, 01/09.
Member, Department of Chemistry Chair Search Committee, 06/2005 – 01/06. (Ortiz)
Graduate Student Recruiter, Southeast Regional Meeting of the American Chemical Society (SERMACS), Raleigh 11/04, Atlanta 11/03, Charleston 11/02, Savannah 09/01.
Member, Biological NMR Faculty Search Committee, 08/03 – 12/04. (Mohanty)
Organizer, State University of West Georgia REU Visit to Auburn Chemistry and Biochemistry, 12 undergraduates, 1 faculty, 06/13/03.
Chair, Biochemistry Faculty Search Committee, 07/01 – 05/02. (Duin)
Chair, Biomacromolecular Crystallography Faculty Search Committee, 07/00 – 05/01.
Member, Biochemistry Faculty Search Committee, 07/00 – 05/01. (Ellis)
Member, Biochemistry Faculty Search Committee, 08/99 – 05/00).
Academic Advisor, Biochemistry Majors, Chemistry and Biochemistry, 08/00 – 05/17.
Academic Advisees
Major |
Students (46
total) |
Biochemistry |
Jessica Andry, Daniel Arias, Austin Arnold, Kendal Benson, Christy Bronaugh, Matthew Brown, Bryan Cronin, Jennifer Falls, Eric Funderburg, Carmen Gaines, Grayson Gladdish, Timothy Guice, Morgan Gwynn, Kathryn Heflin, Kristen Hertwig, Graham Johnson, Kelly Lynn, Cecilia Masucci, Matthew McDonald, Walter Meadows, JaRyce Nabors, Natasha Narayanan, Mary O’Barr, Aseba Okim, Thomas |
Parish, Sarah Peaslee, Alexander Pilgreen, John Rinker, Bailey Roberts, Tyler Sharp, Gary Sheffield, Daniel Smith, Tanner Smith, Molly Smithers, Andrew Stephens, Ashleigh Stokes, Cameron Terrell, Ryan Tucker, William Walraven, Rachel Williams, Landon Wilson, Carl Worley, Jeffery Zaballa |
|
|
|
Chemistry |
Jenny Alexander, David Hagins |
|
|
Molecular Biology |
Emily Brantley |
4.D.a.2. COSAM Service:
Member, COSAM
Biomedical Sciences Curriculum Review Committee (August 2023 – present)
Member, COSAM
Executive Team (07/20 – present)
Member, COSAM Biomedical
Sciences Leadership Review Committee (January – May 2023)
Chair, COSAM Associate
Dean for Research and Graduate Affairs Search Committee (March – April 2023)
Member, COSAM Acting
Deputy Associate Dean for Academic Affairs Search Committee (April – May 2022)
Member, COSAM Acting
Associate Dean for Research Search Committee (July 2021)
Member, COSAM Dean Search Committee (August 2021 – April
2022)
Member,
COSAM Dean Search Committee
(November 2020 – April 2021)
Member, Cellular and Molecular Biosciences Program
Graduate Fellowship Committee (Spring 2007, Spring 2008, Spring 2009).
Member, Dean’s Research Awards Committee (08/06 – 05/09)
Member, COSAM Leaders Faculty/Student Interview Panel, 04/04, 04/05 04/07, 04/08.
Member, Biological NMR Symposium Organizing Committee, 08/02 – 05/03.
4.D.a.3. University Service
Member, Advisory Council, Alabama Prison Arts +
Education Project, 09/15 – present.
Senator, Chemistry and Biochemistry representative to the University Senate, 07/15 – 07/20.
Member, Project Coordinator Search Committee, Alabama Prison Arts + Education project, 09/16 – 04/17.
Member, Ad Hoc Mock Interview Panel, Gates-Cambridge Finalist, 01/14 – 02/14.
Faculty Representative, Camp War Eagle Session 4, 06/25/15 – 06/26/15.
4.D.b. Professional Service
Program Chair, 11th Annual Southeast Enzyme
Conference, originally scheduled May 16, 2020 and
postponed to April 10, 2021, Virtual.
Reviewer, Biochemistry, Journal of the American Chemical Society, Biochimica et Biophysica Acta, General Subjects, Biochimica et Biophysica Acta, Proteins and Proteomics, Journal of Biological Inorganic Chemistry, Biochemie, Journal of Inorganic Biochemistry, Journal of Biological Chemistry, Chemical Research in Toxicology, Biophysical Chemistry, PLOS One, Proceedings of the National Academy of Sciences, Phytochemistry Reviews, Bioorganic and Medicinal Chemistry, Applied Microbiology, International Journal of Chemical Kinetics
Ad Hoc Reviewer (2007 - present), National Science Foundation
Lead Panelist, National
Science Foundation, Metabolic Biochemistry Panel, Fall 2009 – four proposals.
Secondary Panelist, National Science Foundation,
Metabolic Biochemistry Panel, Fall 2009 – four proposals.
Scribe Panelist, National Science Foundation, Metabolic
Biochemistry Panel, Fall 2009 – four proposals.
Lead Panelist, National Science Foundation, Metabolic
Biochemistry Panel, Fall 2008 – six proposals.
Secondary Panelist, National Science Foundation, Metabolic
Biochemistry Panel, Fall 2008 – six proposals.
Session Chair, Fifth
Southeast Enzymes Conference, Atlanta, GA, 04/05/14
Treasurer, American Chemical Society, Auburn Section,
02/00 – 03/04
Member, American Chemical Society, Division of Biological Chemistry
Member, American Society for Biochemistry and Molecular Biology
4.D.c. Other
Letters, because I teach courses with large numbers of undergraduate students close to graduation, I write a very large number of recommendation letters every year. Over the last seven years, I have written 536 letters for 234 different students and colleagues.