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
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
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
Moore, R.L., Powell, L.J., and Goodwin, D. C. 2008. The
kinetic properties producing the perfunctory pH profiles of
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,
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,
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,
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.