PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17252785-6 2006 Cobalt-impregnated Fe-MCM-41 (Co/Fe = 1) produced a small fraction of SWNTs of ca. Cobalt 0-6 methylmalonyl-CoA mutase Homo sapiens 22-25 9132024-0 1997 Evidence that cobalt-carbon bond homolysis is coupled to hydrogen atom abstraction from substrate in methylmalonyl-CoA mutase. Cobalt 14-20 methylmalonyl-CoA mutase Homo sapiens 101-125 10924114-1 2000 Adenosylcobalamin-dependent methylmalonyl-CoA mutase catalyzes the interconversion of methylmalonyl-CoA and succinyl-CoA via radical intermediates generated by substrate-induced homolysis of the coenzyme carbon-cobalt bond. Cobalt 211-217 methylmalonyl-CoA mutase Homo sapiens 28-52 9242908-2 1997 These structures reveal that the B12 cofactor undergoes a major conformational change on binding to the apoenzymes of methionine synthase and methylmalonyl-coenzyme A mutase: The dimethylbenzimidazole ligand to the cobalt is displaced by a histidine residue from the protein. Cobalt 215-221 methylmalonyl-CoA mutase Homo sapiens 142-173 9242908-8 1997 The best-characterized B12-dependent mutases that catalyze carbon skeleton rearrangement, for which methylmalonyl-coenzyme A mutase is the prototype, also bind cobalamin cofactors with histidine as the cobalt ligand, although other cobalamin-dependent mutases do not appear to utilize histidine ligation. Cobalt 202-208 methylmalonyl-CoA mutase Homo sapiens 100-131 30282455-3 2018 If methylmalonyl-CoA mutase is unavailable to accept the coenzyme B12 product of adenosyltransferase, the latter catalyzes homolytic scission of the cobalt-carbon bond in an unconventional reversal of the nucleophilic displacement reaction that was used to make it. Cobalt 149-155 methylmalonyl-CoA mutase Homo sapiens 3-27 31672889-5 2019 Crystallography and spectroscopy of the inhibited enzyme are consistent with a metal-centered cobalt radical ~6 angstroms away from the tertiary carbon-centered radical and suggest a means of controlling radical trajectories during MCM catalysis. Cobalt 94-100 methylmalonyl-CoA mutase Homo sapiens 232-235