Faculty

David Goodin 
Associate Professor
Department of Molecular Biology
TSRI - 1987

Education 
Ph. D., University of California, Berkeley, 1983

Awards & Activities 
Review panels: 1994, NIH Study Section, Biomedical Research Technology Resource; 1997, NIH Study Section, Physical Biochemistry; 1999-2003, NIH Study Section, Metallobiochemistry.



Recent Invited lectures (2000-2002): XIX Congress of the International Union of Crystallography, Geneva; Gordon Conference on Tetrapyrroles, Salve Regina; American Chemical Society, San Diego; XIX International Conference on Magnetic Resonance in Biological Systems, Florence, Italy; University of Pennsylvania; University of North Carolina, Chapel Hill, University of North Dakota; University of Illinois, Champaign-Urbana.

Research Focus 
Our research is focused on rational engineering of the structures of metalloenzyme catalysts in order to better understand the chemical diversity of natural enzymes and to generate novel catalysts of potential utility. We use a multidisciplinary approach combining spectroscopic and biophysical methods with X-ray crystallography. One of the approaches we have developed is the use of cavity complementation or chemical rescue to introduce binding sites for small molecules at specific locations within a protein. Engineered small molecule sites can be positioned relative to the active site to enable one of several types of oxidative catalysis, including the delivery of activated oxygen to alkenes, promotion of electron transfer by transition state stabilization, or new electron transfer pathways from redox active metal centers.

Selected References 
Hirst, J., and Goodin, D. B.(2000) "Unusual oxidative chemistry of Nw-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase", J Biol. Chem. 275, 8582-8591.

Hirst, J., Wilcox, S. K., Williams, P. A., Blankenship, J., McRee, D. E., and Goodin, D. B. (2001) "Replacement of the Axial Histidine Ligand with Imidazole in Cytochrome c Peroxidase. 1. Effects on Structure", Biochemistry 40, 1265-1273.

Musah, R. A., Jensen, G. M., Bunte, S. W., Rosenfeld, R. J., and Goodin, D. B. (2002) "Artificial Protein Cavities as Specific Ligand-Binding Templates: Characterization of an Engineered Heterocyclic Cation Binding Site that Preserves the Evolved Specificity of the Parent Protein", Journal of Molecular Biology, in press.

Rosenfeld, R. J., Hays, A.-M. A., Musah, R. A., and Goodin, D. B. (2002) "Excision of a proposed electron transfer pathway in cytochrome c peroxidase and its replacement by a ligand-binding channel", Protein Science, in press.