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Jeffrey Bolin Publications


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: 36377-36385.

Gomez-Gil, L., Kumar, P., Barriault, D., Bolin, J. T., Sylvestre, M., Eltis, L. D. 2007. Characterization of biphenyl dioxygenase of Pandoraea pnomenusa B-356 as a potent polychlorinated biphenyl-degrading enzyme. J Bacteriol. 189: 5705-5715.

Horsman, G. P., Bhowmik, S., Seah, S. Y., 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: 19894-19904.

Horsman, G. P., Ke, J., Dai, S., Seah, S. Y., 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: 11071-11086.

Vaillancourt, F. H., Bolin, J. T., Eltis, L. D. 2006. The ins and outs of ring-cleaving dioxygenases. Crit Rev Biochem Mol Biol. 41: 241-267.

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: 42307-42314.

Davis, M. I., Wasinger, E. C., Decker, A., Pau, M. Y., Vaillancourt, F. H., Bolin, J. T., Eltis, L. D., Hedman, B., Hodgson, K. O., Solomon, E. I. 2003. Spectroscopic and electronic structure studies of 2,3-dihydroxybiphenyl 1,2-dioxygenase: O2 reactivity of the non-heme ferrous site in extradiol dioxygenases. J Am Chem Soc. 125: 11214-11227.

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. Nat Struct Biol. 9: 934-939.

Vaillancourt, F. H., Barbosa, C. J., Spiro, T. G., Bolin, J. T., Blades, M. W., Turner, R. F., Eltis, L. D. 2002. Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography. J Am Chem Soc. 124: 2485-2496.

Couture, M. M., Colbert, C. L., Babini, E., Rosell, F. I., Mauk, A. G., Bolin, J. T., Eltis, L. D. 2001. Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential. Biochemistry. 40: 84-92.

Low, P. S., Zhang, D., Bolin, J. T. 2001. Localization of mutations leading to altered cell shape and anion transport in the crystal structure of the cytoplasmic domain of band 3. Blood Cells Mol Dis. 27: 81-84.

Colbert, C. L., Couture, M. M., Eltis, L. D., Bolin, J. T. 2000. A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure. 8: 1267-1278.

Imbeault, N. Y., Powlowski, J. B., Colbert, C. L., Bolin, J. T., Eltis, L. D. 2000. Steady-state kinetic characterization and crystallization of a polychlorinated biphenyl-transforming dioxygenase. J Biol Chem. 275: 12430-12437.

Zhang, D., Kiyatkin, A., Bolin, J. T., Low, P. S. 2000. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood. 96: 2925-2933.

Crabb, W. D., Bolin, J. 1999. Protein technologies and commercial enzymes. Current Opinion in Biotechnology. 10: 321-323.

Bergdoll, M., Eltis, L. D., Cameron, A. D., Dumas, P., Bolin, J. T. 1998. All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci. 7: 1661-1670.

Seah, S. Y., Terracina, G., Bolin, J. T., Riebel, P., Snieckus, V., Eltis, L. D. 1998. Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls. J Biol Chem. 273: 22943-22949.

Eltis, L. D., Bolin, J. T. 1996. Evolutionary relationships among extradiol dioxygenases. J Bacteriol. 178: 5930-5937.

Minor, W., Steczko, J., Stec, B., Otwinowski, Z., Bolin, J. T., Walter, R., Axelrod, B. 1996. Crystal structure of soybean lipoxygenase L-1 at 1.4 A resolution. Biochemistry. 35: 10687-10701.

Han, S., Eltis, L. D., Timmis, K. N., Muchmore, S. W., Bolin, J. T. 1995. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science. 270: 976-980.

Bolin, J. T., Ronco, A. E., Morgan, T. V., Mortenson, L. E., Xuong, N. H. 1993. The unusual metal clusters of nitrogenase: structural features revealed by x-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum. Proc Natl Acad Sci U S A. 90: 1078-1082.

Chen, J, Christiansen, J, Campobasso, N, Bolin, JT, Tittsworth, RC, Hales, BJ, Rehr, JJ, Cramerr, SP. 1993. Refinement of a Model for the Nitrogenase MoFe Cluster Using Single Crystal Mo and Fe EXAFS. Angew. Chem. Intl. Ed.. 32: 1592-1594.

Dean, D. R., Bolin, J. T., Zheng, L. 1993. Nitrogenase metalloclusters: structures, organization, and synthesis. J Bacteriol. 175: 6737-6744.

Minor, W., Steczko, J., Bolin, J. T., Otwinowski, Z., Axelrod, B. 1993. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. Biochemistry. 32: 6320-6323.

Mortenson, L. E., Seefeldt, L. C., Morgan, T. V., Bolin, J. T. 1993. The role of metal clusters and MgATP in nitrogenase catalysis. Adv Enzymol Relat Areas Mol Biol. 67: 299-374.

Christiansen, J., Chen, J., George, S. J., Cramer, S. P., Campobasso, N., Bolin, J., George, G. N. 1992. Polarized Iron Exafs of Single-Crystal Nitrogenase. 203: 600-INOR.

Cramer, S. P., Chen, J., George, S., Christiansen, J., Vanelp, J., Tittsworth, R., Hales, B., Smith, B., Coucouvanis, D., Campobasso, N., Bolin, J. 1992. X-Ray Spectroscopy of Nitrogenase Femo Protein. 204: 116-INOR.

Ray, W. J., Jr., Bolin, J. T., Puvathingal, J. M., Minor, W., Liu, Y. W., Muchmore, S. W. 1991. Removal of salt from a salt-induced protein crystal without cross-linking. Preliminary examination of "desalted" crystals of phosphoglucomutase by X-ray crystallography at low temperature. Biochemistry. 30: 6866-6875.

Brunie, S., Bolin, J., Gewirth, D., Sigler, P. B. 1985. The refined crystal structure of dimeric phospholipase A2 at 2.5 A. Access to a shielded catalytic center. J Biol Chem. 260: 9742-9749.

Matthews, D. A., Bolin, J. T., Burridge, J. M., Filman, D. J., Volz, K. W., Kaufman, B. T., Beddell, C. R., Champness, J. N., Stammers, D. K., Kraut, J. 1985. Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim. J Biol Chem. 260: 381-391.

Matthews, D. A., Bolin, J. T., Burridge, J. M., Filman, D. J., Volz, K. W., Kraut, J. 1985. Dihydrofolate reductase. The stereochemistry of inhibitor selectivity. J Biol Chem. 260: 392-399.

Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C., Kraut, J. 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. J Biol Chem. 257: 13650-13662.

Filman, D. J., Bolin, J. T., Matthews, D. A., Kraut, J. 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis. J Biol Chem. 257: 13663-13672.

Matthews, D. A., Alden, R. A., Bolin, J. T., Freer, S. T., Hamlin, R., Xuong, N., Kraut, J., Poe, M., Williams, M., Hoogsteen, K. 1977. Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate. Science. 197: 452-455.

Bowie, L., Esters, F., Bolin, J., Gochman, N. 1976. Development of an aqueous temperature-indicating technique and its application to clinical laboratory instrumentation. Clin Chem. 22: 449-455.

Book Section

Bolin, JT, Campobasso, N, Muchmore, SW, Minor, W, Morgan, TV, Mortenson, LE. 1993. The Crystal Structure of the Nitrogenase MoFe-protein from Clostridium pasteurianum. 89-94.


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