Vanderbilt University

Richard N. Armstrong, Ph.D.

Richard N. Armstrong Ph.D.Professor of Biochemistry and Chemistry

Ph.D., Marquette University, 1975 (Organic Chemistry)

Research efforts are focused on elucidating the mechanisms of action of enzymes involved in the metabolism of foreign compounds. The relationship between the molecular structure and catalytic function of several enzymes, including glutathione transferases and epoxide hydrolases, is being evaluated in an effort to understand how detoxication enzymes cooperate in the metabolism of foreign molecules. A second aim is to understand the enzymology of antibiotic resistance in microorganisms. Microbial resistance to current therapeutic strategies is a serious and fundamental challenge to the control of infectious disease. Current studies are designed to pave the way for new, more effective antimicrobial agents.


Recent Publications

Fillgrove KL, Pakhomova S, Schaab MR, Newcomer ME, Armstrong RN. Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes. Biochemistry. 2007 46:8110-20.

Thompson LC, Ladner JE, Codreanu SG, Harp J, Gilliland GL, Armstrong RN. 2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida. Biochemistry. 2007 46:6710-22.

Busenlehner LS, Alander J, Jegerscohld C, Holm PJ, Bhakat P, Hebert H, Morgenstern R, Armstrong RN. Location of substrate binding sites within the integral membrane protein microsomal glutathione transferase-1. Biochemistry. 2007 46:2812-22.

Busenlehner LS, Salomonsson L, Brzezinski P, Armstrong RN. Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase. Proc Natl Acad Sci U S A. 2006 103:15398-403.

Thompson LC, Walters J, Burke J, Parsons JF, Armstrong RN, Dirr HW. Double mutation at the subunit interface of glutathione transferase rGSTM1-1 results in a stable, folded monomer. Biochemistry. 2006 45:2267-73.