Journal
CHEMICAL PHYSICS LETTERS
Volume 386, Issue 1-3, Pages 174-178Publisher
ELSEVIER
DOI: 10.1016/j.cplett.2004.01.048
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Density functional theory B3LYP calculations have been carried out on a large model for coenzyme B-12. The dissociation curve for the homolytic cleavage of the Co-C bond has been studied for the free cofactor, in the gas phase and including the effect of a dielectric continuum with a dielectric constant of 4.00, as well as in the presence of some key residues present in methylmalonyl-CoA mutase, an enzyme that depends on coenzyme B-12. We describe a hitherto unknown effect of the cofactor which facilitates the homolysis reaction: electrostatic interactions stabilize the radicals formed in this step. H-bonding to protein residues leads to further stabilization. (C) 2004 Elsevier B.V. All rights reserved.
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