Professor Kurtz received his B.S. from the University of Akron in 1972 and his Ph.D. from Northwestern University in 1977. He was an NIH Postdoctoral Fellow at Stanford University and Assistant Professor at Iowa State University before joining the Georgia faculty in 1986. He was an NIH Research Career Development Awardee during 1988-1993. His research interests are in the area of bioinorganic chemistry.
We are interested in understanding the molecular determinants of the structure and function of non-heme iron proteins. Our present approach to this goal incorporates interdisciplinary training in inorganic chemistry, spectroscopy, biochemistry, and molecular biology. We have cloned and overexpressed several non-heme iron proteins, and have mutated specific amino acid residues in order to systematically alter the structure and reactivity of the m etal sites. Rubrerythrin, a protein from anaerobic sulfate-reducing bacteria, has the ability to catalyze oxidation of Fe2+ to Fe3+ by O2. This protein contains both FeS4 and diiiron-oxo sites. Using the techniques of modern molecular biology, we have created a mutated variant of rubrerythrin which contains only the diiron domain, allowing us to study the structure and function of the diiron-oxo site in more detail than previously possible. We are also developing the non-heme iron protein, hemerythrin, as a O2-carrying protein for use in blood substitutes. Thus, we expect our research to evolve into the rational design of metalloproteins having well-defined structures and functions, i.e., a sort of inorganic biosynthesis.
N. Gupta, F. Bonomi, D.M. Kurtz, Jr., N. Ravi, D.L. Wang and B.H. Huynh, "Recombinant Desulfovibrio vulgaris Rubrerythrin. Isolation and Characterization of the Diiron Domain", Biochemistry 1995, 34, 3310.
D.M. Kurtz, Jr., "Iron Proteins with Dinuclear Active Sites" , in Encyclopedia of Inorganic Chemistry, Vol. 4, R.B. King, ed.,Wiley, Chichester, pp. 1847-1859, 1994.