COSAM » COSAM Faculty » Faculty & Staff » Doug Goodwin

Doug Goodwin
Chemistry and Biochemistry
Associate Professor

Research Areas - Biochemistry

Address:
179 Chemistry Building
Auburn, AL 36849

Phone: (334) 844-6992
Fax: (334) 844-6959
E-Mail: goodwdc@auburn.edu

Research Page


Education

Ph.D., Utah State University
1996
B.A., University of Northern Colorado
1991


Professional Employment

Associate Professor, Department of Chemistry and Biochemistry, Auburn University
2002 - present
Assistant Professor, Department of Chemistry and Biochemistry, Auburn University
1999 - 2005
Post-doctoral Fellow, Vanderbilt University
1996 - 1999


Honors and Awards

Department of Chemistry and Biochemistry Nominee for Auburn University Award for Excellence in Faculty Outreach. Department of Chemistry and Biochemistry, Auburn University
2015
Department of Chemistry and Biochemistry Nominee for COSAM Faculty Outreach Award Department of Chemistry and Biochemistry, Auburn University
2015
Department of Chemistry and Biochemistry Nominee for Auburn University Award for Excellence in Faculty Outreach. Department of Chemistry and Biochemistry, Auburn University
2014
American Chemical Society Outreach Volunteers of the Year . Auburn Section of the American Chemical Society
2014
American Chemical Society Outreach Volunteers of the Year, Auburn Section of the American Chemical Society
2014
Final Lecture Nominee. SGA-sponsored student-nominated award selected by campus-wide vote of the students. Auburn University
2014
Nominee for Auburn University Alumni Association Undergraduate Teaching Excellence Award. Student - initiated nomination, Auburn University
2013
College of Sciences and Mathematics Outstanding Teacher Award, Auburn University
2011
Alpha Epsilon Delta Honorary National Membership, Awarded by the Auburn University AED Chapter
2011
Golden Key National Honor Society Teaching Award , Golden Key Honor Society, Auburn University Chapter
2011
Treasurer: Auburn Section of the American Chemical Society, Auburn, AL
2000 - 2004
E.L. and Inez Waldron Award , Biotechnology Center, Utah State University
1996
George H. and Billie Bush Emert Scholar, Department of Chemistry and Biochemistry, Utah State University
1996
Thomas F. Emery Memorial Research Scholar, Department of Chemistry and Biochemistry, Utah State University
1995


Professional Activities

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: National Science Foundation (2007 - present)
Lead Panelist: National Science Foundation, Metabolic Biochemistry Panel, Fall 2009 - four proposals
Secondary Panelist: Ntional 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
Treasurer: American Chemical Society, Auburn Section, 2000 - 2004


Research and Teaching Interests

Biochemistry:  Structure and function of heme-dependent enzymes

Our laboratory is interested in the relationship between an enzyme’s structure and its catalytic function in biological systems.  In particular, we focus on enzymes that require the organometallic cofactor heme in order to function.  Heme is used by a surprisingly broad range of enzymes to accomplish an equally broad range of biologically essential tasks.  For example, these enzymes are central to metabolizing foreign compounds, safely disposing of H2O2 (a toxic side product of aerobic metabolism), and mounting an effective immune response.  In spite of the many and very different functions accomplished by heme-dependent enzymes, each of them relies on this organometallic molecule to accomplish the job.  Clearly, the protein structure surrounding the heme group is what dictates the unique catalytic abilities of each heme-dependent enzyme.

KatG dimer (ribbons and surface)The Goodwin laboratory is using a group of bacterial enzymes called catalase-peroxidases to shed light on a poorly understood but very important aspect of the heme enzyme structure/function equation.  Using these enzymes, we are demonstrating that structural components quite distant from the active site heme have a critical role in directing and fine-tuning the catalytic capabilities of heme enzymes.  Not only does our research answer fundamental questions about the nature of catalysis in biological systems, but it also provides specific insight that is foundational for technological advances through enzyme engineering.  The ability to engineer new enzymes for unique functions holds great promise for addressing urgent concerns that are global in their scope and impact (e.g., contamination of the environment by toxic pollutants).

Our research also has implications for and applications toward substantial biomedical concerns, including antibiotic resistance and bacterial virulence.  Catalase-peroxidase from Mycobacterium tuberculosis has been exploited for the activation of the front-line antitubercular agent isoniazid to its antibiotic form.  Interestingly, the increasing prevelance of isoniazid resistant M. tuberculosis is strongly tied (over 70% of resistant strains) to mutations that compromise the ability of catalase-peroxidase to catalyze activation. Furthermore, a group of catalase-peroxidases have been identified as potential virulence factors in pathogens such as Escherichia coli strain O157:H7 and Yersinia pestis, both of which are recognized as high priority threats as agents of bioterrorism.  Nevertheless, how these enzymes may operate as virulence factors has not been illuminated.  Clearly, there are important benefits to be derived from understanding the structure and function of the catalase-peroxidases.



Selected Publications

  • Kudalkar, S.N.; Njuma, O.J.; Li, Y.; Muldowney, M.; Fuanta, N.R.; Goodwin, D.C. "A role for catalase-peroxidase large loop 2 revealed by deletion mutagenesis: Control of active site water and ferric enzyme reactivity" Biochemistry 201554, 1648.
  • Simithy, J.; Gill, G.; Wang, Y.; Goodwin, D.C.; Calderón, A.I. "Development of an ESI-LC-MS based assay for kinetic evaluation of M. tuberculosis shikimate kinase" Anal. Chem. 201587, 2129.
  • Huang, J.; Smith, F., Panizzi, J.R.; Goodwin, D.C.; Panizzi, P. "Inactivation of myeloperoxidase by benzoic acid hydrazide" Arch. Biochem. Biophys2015570, 14.
  • McCarty, S.E.; Schellenberger, A.; Goodwin, D.C.; Fuanta, N.R.; Tekwani, B.L.; Calderón, A.I. "Plasmodium falciparum thioredoxin reductase (PfTrxR) and its role as a target for new antimalarial discovery" Molecules201520, 11459.
  • Njuma, O.J.; Ndontsa, E.N.; Goodwin, D.C.  "Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG" Arch. Biochem. Biophys. 2014544, 27.
  • Wang, Y.; Goodwin D.C.  "Integral role of the I'-helix in the function of the "inactive" C-terminal domain of catalase-peroxidase (KatG)" Biochim. Biophys. Acta 20131834, 362.
  • Kudalkar, S.N.; Campbell, R.A.; Li, Y.; Varnado, C.L.; Prescott, C.; Goodwin, D.C.  "Enhancing the peroxidatic activity of KatG by deletion mutagenesis" J. Inorg. Biochem. 2012116, 106.
  • Ndontsa, E.N.; Moore, R.L.; Goodwin, D.C.  "Stimulation of KatG catalase activity by peroxidatic electron donors"  Arch. Biochem. Biophys. 2012105, 215.






Last updated: 05/26/2016