Unusual Aerobic Stabilization of Cob(I)alamin by a B-12-Trafficking Protein Allows Chemoenzymatic Synthesis of Organocobalamins

作者：Li Zhu; Lesniak Nicholas A; Banerjee Ruma^*

来源：Journal of the American Chemical Society, 2014, 136(46): 16108-16111.

DOI：10.1021/ja5077316

CblC, a B-12 trafficking protein, exhibits glutathione transferase and reductive decyanase activities for processing alkylcobalamins and cyanocobalamin, respectively, to a common intermediate that is subsequently converted to the biologically active forms of the cofactor. We recently discovered that the Caenorhabditis elegans CblC catalyzes thiol-dependent decyanation of CNCbl and reduction of OH(2)Cbl and stabilizes the paramagnetic cob(II)alamin product under aerobic conditions. In this study, we report the striking ability of the worm CblC to stabilize the highly reactive cob(I)alamin product of the glutathione transferase reaction. The unprecedented stabilization of the supernucleophilic cob(I)alamin species under aerobic conditions by the intrinsic thiol oxidase activity of CblC, was exploited for the chemoenzymatic synthesis of organocobalamin derivatives under mild conditions.

• 出版日期2014-11-19