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• W2005508155 abstract "A combined density functional theory (DFT) and molecular mechanics (MM) approach was applied to investigate the relationship between the structure of a free coenzyme B12, and bound to methylmalonyl-CoA mutase. It was found that, upon coenzyme binding to apoenzyme, the Co-C bond remains intact, while the C-Naxial bond becomes slightly elongated and labilized. The labilization of the Co-Naxial bond that takes place in coenzyme B12-dependent enzymes is most likely necessary for fine-tuning of the cobalt-nitrogen (axial base) distance. The controlling of this distance is important to inhibit abiological site reaction involving heterolysis of the Co-C bond but is not important for biologically relevant Co-C bond homolysis." @default.
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• W2005508155 date "2004-01-28" @default.
• W2005508155 modified "2023-09-27" @default.
• W2005508155 title "A Combined Density Functional Theory and Molecular Mechanics Study of the Relationship between the Structure of Coenzyme B12 and Its Binding to Methylmalonyl-CoA Mutase" @default.
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• W2005508155 doi "https://doi.org/10.1021/ja028473o" @default.
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