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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.
Selected Publications:
Dai, S., Vaillancourt, F.H., Maaroufi, H., Drouin, N.M., Neau, D.B., Snieckus, V., Bolin, J.T. & Eltis, L.D. (2002) Identification and analysis of a bottleneck in PCB biodegradation. Nature Struct. Biol. 9: 934-9
Fortin, P.D., MacPherson, I., Neau, D.B., Bolin, J.T. & Eltis, L.D. (2005) Directed evolution of a ring-cleaving dioxygenase for polychlorinated biphenyl degradation. J. Biol. Chem. 280: 42307-14
Horsman, G.P., Ke, J.Y., Dai, S.D., Seah, S.Y.K., Bolin, J.T. & Eltis, L.D. (2006) Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway. Biochemistry 45: 11071-86
Horsman, G.P., Bhowmik, S., Seah, S.Y.K., Kumar, P., Bolin, J.T. & Eltis, L.D. (2007) The tautomeric half-reaction of BphD, a C-C bond hydrolase - Kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triad. J. Biol. Chem. 282: 19894-904
Bhowmik, S., Horsman, G.P., Bolin, J.T. & Eltis, L.D. (2007) The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in polychlorinated biphenyls degradation - Large 3-substituents prevent tautomerization. J. Biol. Chem. 282: 36377-85
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