Among the coenzyme B₁₂-dependent enzymes, methylmalonyl-CoA mutase (MMCM) catalyzes the carbon-skeleton rearrangement reaction between R-methylmalonyl-CoA and succinyl-CoA. Diethyl 2-bromomethyl-2-phenylmalonate, an alkyl bromide substrate having two different migrating groups (phenyl and carboxylic ester groups) on the β-carbon, was applied to the electrolysis mediated by a hydrophobic vitamin B₁₂ model complex, heptamethyl cobyrinate perchlorate in this study. The electrolysis of the substrate at − 1.0 V vs. Ag-AgCl by light irradiation afforded the simple reduced product (diethyl 2-methyl-2-phenylmalonate) and the phenyl migrated product (diethyl 2-benzyl-2-phenylmalonate), as well as the electrolysis of the substrate at − 1.5 V vs. Ag-AgCl in the dark. The electrolysis of the substrate at − 2.0 V vs. Ag-AgCl afforded the carboxylic ester migrated product (diethyl phenylsuccinate) as the major product. The selectivity for the migrating group was successfully tuned by controlling the electrolysis potential. We clarified that the cathodic chemistry of the Co(III) alkylated heptamethyl cobyrinate is critical for the selectivity of the migrating group through mechanistic investigations and comparisons to the simple vitamin B₁₂ model complex, an imine/oxime-type cobalt complex.

在辅酶B ₁₂依赖性酶中，甲基丙二酰-CoA突变酶（MMCM）催化R-甲基丙二酰-CoA和琥珀酰-CoA之间的碳骨架重排反应。将2-溴甲基-2-苯基丙二酸二乙酯（一种在β碳上具有两个不同迁移基团（苯基和羧酸酯基）的烷基溴化物底物）用于由疏水性维生素B ₁₂模型配合物（高氯酸七甲酯）形成的电解溶液。这项研究。基板在-1.0 V vs.Ag-AgCl通过光照射得到简单的还原产物（2-甲基-2-苯基丙二酸二乙酯）和苯基迁移产物（2-苄基-2-苯基丙二酸二乙酯），以及在-1.5 V vs. 。银-氯化银在黑暗中。相对于Ag-AgCl，在-2.0 V下对底物进行电解，得到羧酸酯迁移产物（苯基琥珀酸二乙酯）作为主要产物。通过控制电解电位成功地调节了迁移基团的选择性。我们通过机械研究和与简单维生素B _12的比较，阐明了Co（III）烷基化的七甲基七丁香酸酯的阴极化学对于迁移基团的选择性至关重要。 模型复合物，一种亚胺/肟型钴复合物。