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PULSe Home > Faculty Members A-C > Jeffrey Bolin
Jeffrey T. Bolin
Current Research Interests:
Our research centers on defining relationships between the three-dimensional structures of proteins and their functions through the application of X-ray crystallography in combination with other biophysical and biochemical methods. We focus on studies of metalloenzymes because of their special abilities to catalyze difficult reactions. One current project involves enzymes involved in the biodegradation of aromatic and haloaromatic compounds, a process that has potential applications in the bioremediation of deleterious pollutants. To facilitate adaptation of microbial pathways to this use, as well as to understand the chemistry of the reactions involved, we are investigating the enzymes involved in the degradation of biphenyl and polychlorinated biphenyls (PCBs). We recently determined the crystal structure of the extradiol dioxygenase that catalyzes the critical ring-cleavage step in the degradation of biphenyl and PCBs; this first high resolution structure of any extradiol dioxygenase led to detailed studies of the evolution of homologous enzymes of both similar and divergent functions. Current efforts target enzymes that catalyze other steps in the same and related pathways. A primary focus has been the multiprotein biphenyl dioxygenase system, which catalyzes the initial step in the pathway. As part of his BMB thesis research, Chris Colbert has analyzed the structures of BPDO, the dioxygenase component, and BphF, a Rieske-type ferredoxin that serves as its electron donor. The former structure rationalizes the inability of the enzyme to process certain PCBs, whereas the latter provides a very interesting example of the influence of protein structure on the electrochemical properties of metal-sulfur clusters.
Selected Publications:
Han, S., L. D. Eltis, K. N. Timmis, S. W. Muchmore, and J. T. Bolin. 1995. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 290: 976-980.
Bergdoll, M., L. D. Eltis, A. D. Cameron, P. Dumas, and J. T. Bolin. 1998. All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.Protein Sci. 7: 1661-1670.
Colbert, C. L., M. M.-J. Couture, L. D. Eltis, and J. T. Bolin. 2000. A cluster exposed: crystal structure of the Rieske ferredoxin from biphenyl dioxygenase and determinants of the redox properties of Rieske FeS proteins. Structure in press.
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