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|Title:||Co 2+ /Co + redox tuning in methyltransferases induced by a conformational change at the axial ligand||Authors:||Kozlowski, Pawel M.
|Issue Date:||2012||Source:||Kumar, M., Kumar, N., Hirao, H., & Kozlowski, P. M. (2012). Co 2+ /Co + Redox Tuning in Methyltransferases Induced by a Conformational Change at the Axial Ligand. Inorganic Chemistry, 51(10), 5533-5538.||Series/Report no.:||Inorganic chemistry||Abstract:||Density functional theory and quantum mechanics/molecular mechanics computations predict cob(I)alamin (Co+Cbx), a universal B12 intermediate state, to be a pentacoordinated square pyramidal complex, which is different from the most widely accepted viewpoint of its tetracoordinated square planar geometry. The square pyramidality of Co+Cbx is inspired by the fact that a Co+ ion, which has a dominant d8 electronic configuration, forms a distinctive Co+--H interaction because of the availability of appropriately oriented filled d orbitals. This uniquely H-bonded Co+Cbx may have catalytic relevance in the context of thermodynamically uphill Co2+/Co+ reduction that constitutes an essential component in a large variety of methyltransferases.||URI:||https://hdl.handle.net/10356/96838
|ISSN:||0020-1669||DOI:||10.1021/ic201970k||Rights:||© 2012 American Chemical Society.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||SPMS Journal Articles|
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