Modeling the Active Site of Iron Superoxide Dismutase

Oakland University, Rochester MI

Investigators

Abstract

Ferman Chavez, Department of Chemistry, Oakland University, is supported by the Inorganic, Bioinorganic and Organometallic Chemistry Program for his research program in modeling the active site of iron-dependent superoxide dismutase. The metal-binding site typically contains three nitrogen donors and one oxygen donor derived from the amino acid side chain along with a hydroxide ligand to afford a trigonal bipyramidal geometry. He will design and synthesize organic ligands that mimic this binding site, and then add iron and study the coordination structure and reactivity of the resultant complexes. By studying small molecule models, we can gain insight into metalloenzyme systems. Superoxide dismutase enzymes are ubiquitous in biological systems and protect living systems from the oxidative damage of superoxide by rapidly converting it into oxygen and hydrogen peroxide. Different metals can be involved in this class of enzymes: mammalian enzymes require copper and zinc or manganese while iron-containing superoxide dismutases are found in anaerobic prokaryotes. This award is made under the Minority Research Planning Grant Program and is intended to strengthen the proposal writing and planning capabilities of new investigators and to facilitate preliminary studies and other planning activities related to the research.