Department of Immunology and Microbial Science
The Skaggs Institute for Chemical Biology
Faculty, Graduate Program
We study functionally important protein conformational changes pertinent to protein recognition, interaction and catalysis to provide a detailed understanding of how proteins work. Major research areas include protein photosensing, enzymatic control of reactive oxygen species, the coupling of metal-site chemistry and electron transfer for catalysis, and metalloprotein design. We use multi-wavelength anomalous diffraction; time resolved Laue crystallography; ultra high-resolution protein crystallography; free trapping; femtosecond and nanosecond laser initiation; rapid single-crystal spectroscopy computational and computer graphics analysis; and protein design cycles to test and integrate results from x-ray crystallography, molecular biology, biochemistry, and spectroscopy.
Ph.D., Biochemistry, Duke University, 1982
B.S., Chemistry, Duke University, 1976
Barondeau, D.P., Kassmann, C.J., Tainer, J.A., Getzoff, E.D. (2002). Structural chemistry of a green fluorescent protein Zn biosensor, J. Am. Chem. Soc. 124, 3522-3524.
Forest, K.T., Langford, P.R., Kroll, J.S., and Getzoff, E.D. (2000) Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface, J. Mol. Biol., 296, 145-153.
Brudler, R., Rammelsberg, R. Woo, T.T., Getzoff, E.D., and Gerwert, K. (2001) Stucture of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy. Nature Structural Biology, 8, 265-270.
Aoyagi, M., Arvai, A.S., Ghosh, S., Stuehr, D.J., Tainer, J.A. & Getzoff, E.D. (2001) Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457, Biochemistry, 40, 12826-12832.