Robert Moore

As Robert will gladly confess, he is a native of the Republic of Texas.  Yes.  He is a Dallas Cowboys fan to boot.  We did our best to tolerate such things.  Robert received his bachelor's degree from Huntingdon College in Montgomery, Alabama, where he triple majored in Cell Biology, Chemistry, and Mathematics.  During his time at Huntingdon, Robert was given the Jane T. Williams Freshman Award and the Marion Cantelou Black Chemistry Award.  He was inducted into the Alpha Beta, Beta Beta Beta (Biology), Kappa Mu Epsilon (Mathematics), and Phi Eta Sigma Honor Societies.  Here Robert made an extensive exploration of catalase-peroxidase steady-state kinetics, particularly addressing the pH dependence of each activity as well as substrate-dependent inhibition (also a pH-dependent phenomenon).   He also used  site-directed mutagenesis to disrupt a series of strictly conserved intrasubunit interactions at the interface between the N- and C-terminal domains to evaluate their role in supporting catalase-peroxidase active site function.   Finally, Robert made the initial observations that peroxidatic electron donors stimulate catalase activity.  The effect was modest with E. coli KatG, the enzyme Robert evaluated, but following in his footsteps, Elizabeth Ndontsa noted that M. tuberculosis KatG is particularly responsive to stimulation by peroxidatic electron donors.  In the Summer of 2009, Robert successfully defended his dissertation entitled: Toward the Understanding of Complex Biochemical Systems: The Significance of Global Protein Structure and Thorough Parametric Analysis.  Dr. Moore is now an Associate Professor of Chemistry at Wayland Baptist University in Wayland, TX.

Abstracts, Patents, and Publications

Ndontsa, E.N., Moore, R.L., and Goodwin, D.C.  2012.  Stimulation of KatG catalase activity by peroxidatic electron donors Arch. Biochem. Biophys. 105, 215 - 222.

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 35, (in press).

Cook, C.O., Moore, R.L., and Goodwin, D. C. 2008.  Role of R117 and D597 interdomain residues in the reactivation of E. coli catalase-peroxidase.  American Chemical Society, 235th National Meeting, New Orleans, LA.

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.

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.

Hong, J.W., Goodwin, D.C., Moore, R., and Jambovane, S.  Reaction Kinetic Landscaper.  Invention Disclosure (#06-088) Filed August 31, 2006, Auburn University Technology Transfer Office, U.S. Patent Application No. 60/843,385 filed September 21, 2006.

Moore, R.L., Williams, R., and Goodwin, D.C. 2007.  Role of interdomain interaction of tyrosine 111 on catalase-peroxidase, Southeast Regional Meeting of the American Chemical Society, Greenville, SC.

Cook, C.O., Moore, R.L., Goodwin, D.C. 2007. Effect of distant, intradomain residues on restoring the catalase-peroxidase bifunctional active site, Southeast Regional Meeting of the American Chemical Society, Greenville, SC.

Goodwin, D.C., Cook, C.O., Moore, R.L. 2007.  Roles of distant but highly conserved interactions in maintaining active site function in catalase-peroxidases. Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Biddeford, ME.

Cook, C. O., Moore, R. L., Goodwin, D. C. 2007. Role of intrasubunit interactions between domains in catalase-peroxidase structure and activity. American Chemical Society, 233rd National Meeting, Boston, MA.    

Moore, R., Goodwin, D. C., Laband, K. A., and Powell, L.  2006. Role of interdomain salt bridge on catalase-peroxidase activity.  American Chemical Society, 231st National Meeting, Atlanta, GA.