Donald M. Kurtz Jr.

Donald M. Kurtz, Jr. received his Ph.D. degree at Northwestern University with Irving Klotz in 1977, and did postdoctoral work with Richard Holm on biologically related iron-sulfur chemistry at Stanford University from 1977-79.  He was appointed Assistant Professor of Chemistry at Iowa State University in 1979.  In 1986 he moved to the University of Georgia where he was Associate, Full and Distinguished Research Professor of Chemistry and Biochemistry & Molecular Biology until 2005. From 1987-1993 he was an NIH Research Career Development Awardee. He currently holds the Lutcher Brown Distinguished Chair in the Department of Chemistry at UTSA.

Our research focuses on the structure, function, and catalytic mechanism of bacterial and archaeal non-heme iron enzymes. Anaerobic microorganisms contain enzymes that reductively scavenge molecular oxygen or its reduction products, superoxide and hydrogen peroxide, and also nitric oxide.  These seemingly simple reactions require specialized active sites that contain iron in novel coordination environments and novel mechanisms, which we follow by rapid kinetic and spectroscopic techniques as well as protein X-ray crystallography.  A separate project uses these same techniques to study a group of bacterial non-heme iron enzymes that catalyze aromatic ring dihydroxylation by dioxygen.  A third project focuses on iron storage proteins that catalyze oxidation of intracellular iron and deposits the oxidized iron into a mineral core.

An example of a particularly remarkable mechanistic feature of one these enzymes, which functions as a hydrogen peroxide reductase, is shown below and discussed in reference 2 of Selected Publications.  The red-highlighted iron “toggles” between carboxylate and imidazolyl ligands over a distance of ~2 Å at approximately 30 times per second during catalysis, and this movement occurs even down to 100 K!

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Selected Publications