Influence of equatorial CH⋅⋅⋅O interactions on secondary kinetic isotope effects for methyl transfer

Philippe B. Wilson, Ian H. Williams

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

DFT calculations for methyl cation complexed within a constrained cage of water molecules permit the controlled manipulation of the “axial” donor/acceptor distance and the “equatorial” distance to hydrogen-bond acceptors. The kinetic isotope effect k(CH3)/k(CT3) for methyl transfer within a cage with a short axial distance becomes less inverse for shorter equatorial C⋅⋅⋅O distances: a decrease of 0.5 Å results in a 3 % increase at 298 K. Kinetic isotope effects in AdoMet-dependent methyltransferases may be m∧odulated by CH⋅⋅⋅O hydrogen bonding, and factors other than axial compression may contribute, at least partially, to recently reported isotope-effect variations for catechol-O-methyltransferase and its mutant structures.
Original languageEnglish
Pages (from-to)3244-3247
JournalAngewandte Chemie
Volume128
Issue number9
Early online date28 Jan 2016
DOIs
Publication statusPublished - 24 Feb 2016

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