Abstract
A detailed computational analysis employing density functional theory (DFT), atoms in molecules, and quantum mechanics/molecular mechanics (QM/MM) tools has been performed to investigate the primary coordination environment of cob(I)alamin (Co+Cbx), which is a ubiquitous B12 intermediate in methyltransferases and ATP:corrinoid adenosyltransferases. The DFT calculations suggest that the simplified (Co+Cbl) as well as the complete (Co+Cbi) complexes can adapt to the square pyramidal or octahedral coordination geometry owing to the unconventional H-bonding between the Co+ ion and its axial ligands. These Co+–H bonds contain appreciable amounts of electrostatic, charge transfer, long-range correlation, and dispersion components. The computed reduction potentials of the Co2+/Co+ couple imply that the Co+–H(H2O) interaction causes a greater anodic shift [5–98 mV vs. the normal hydrogen electrode (NHE) in chloroform solvent] than the analogous Co+–H(imidazole) interaction (1 mV vs. NHE) in the reduction potential of the Co2+/Co+ couple. This may explain why a β-axial H2O ligand has specifically been found in the active sites of certain methyltransferases. The QM/MM analysis of methionine synthase bound Co+Cbx (Protein Data Bank ID 1BMT, resolution 3.0 Å) indicates that the enzyme-bound Co+Cbx can also form a Co+–H bond, but can only exist in square pyramidal form because of the steric constraints imposed by the cellular environment. The present calculations thus support a recently proposed alternate mechanism for the enzyme-bound Co2+/Co+ reduction that involves the conversion of square pyramidal Co2+Cbx into square pyramidal Co+Cbx (Kumar and Kozlowski in Angew. Chem. Int. Ed. 50:8702–8705, 2011).
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Notes
Herein Co2+Cbx and Co+Cbx have been used as abbreviations for full cob(II)alamin and cob(I)alamin, respectively. Co2+Cbl and Co+Cbl represent their simplified versions where the corrin side chains as well as the nucleotide loop have been replaced by hydrogens, and Co2+Cbi and Co+Cbi represent their mimics where only the nucleotide loop of the corrin ring has been terminated at the phosphodiester end
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Acknowledgments
H.H. acknowledges a Nanyang assistant professorship for financial support and the High Performance Computing Centre at Nanyang Technological University for computer resources. P.M.K acknowledges the excellent computational facilities provided by the Cardinal Research Cluster at the University of Louisville.
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Kumar, M., Hirao, H. & Kozlowski, P.M. Co+–H interaction inspired alternate coordination geometries of biologically important cob(I)alamin: possible structural and mechanistic consequences for methyltransferases. J Biol Inorg Chem 17, 1107–1121 (2012). https://doi.org/10.1007/s00775-012-0924-x
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DOI: https://doi.org/10.1007/s00775-012-0924-x