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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.
Kumar, Manoj
Kumar, Neeraj
Hirao, Hajime
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.
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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