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Coenzyme B12 and Methyl-B12 Chemistry and Protein Biochemistry |
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In the area of the B12 dependent enzymes, a team of synthetic, biochemical and mechanistic inorganic and organic scientists are working together to better define the mechanisms of this intriguing class of poorly understood enzymes. Obtaining a single crystal X-ray diffraction structural analysis for the B12-dependent enzyme ribonucleotide triphosphate reductase (RTPR) is one important goal. A second important goal is to understand how RTPR’s amazing 1012 activation of Coenzyme B12’s Co-C bond is accomplished at the molecular level. A third important goal is to understand the allosterism of RTPR—purportedly allosterism in a single polypeptide chain. A fourth goal is to provide chemical precedent for the key, elementary steps underlying RTPR’s mechanism of action. A project is also underway, in collaboration with Professor Rowena Matthew’s group at the University of Michigan, to understand the methyl group transfer reactions catalyzed by MeB12-dependent methionine synthase. An initial focus here is to provide chemical precedent for each of the putative elementary steps of methionine synthase. Longer terms goals include kinetic and mechanistic studies with the Matthew’s group of key elementary steps using the various domains of the enzyme methionine synthase that have been developed by the Matthew’s group. |
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 B12 Chemistry |
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