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

11 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

Fingerprint

Isotopes
Catechol O-Methyltransferase
S-Adenosylmethionine
Methyltransferases
Hydrogen Bonding
Cations
Hydrogen
Water

Cite this

Influence of equatorial CH⋅⋅⋅O interactions on secondary kinetic isotope effects for methyl transfer. / Wilson, Philippe B.; Williams, Ian H.

In: Angewandte Chemie, Vol. 128, No. 9, 24.02.2016, p. 3244-3247.

Research output: Contribution to journalArticle

@article{61752a73c074462c9e97a27aed5f3437,
title = "Influence of equatorial CH⋅⋅⋅O interactions on secondary kinetic isotope effects for methyl transfer",
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 {\AA} 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.",
author = "Wilson, {Philippe B.} and Williams, {Ian H.}",
year = "2016",
month = "2",
day = "24",
doi = "10.1002/ange.201511708",
language = "English",
volume = "128",
pages = "3244--3247",
journal = "Angewandte Chemie",
issn = "0044-8249",
publisher = "John Wiley and Sons Inc.",
number = "9",

}

TY - JOUR

T1 - Influence of equatorial CH⋅⋅⋅O interactions on secondary kinetic isotope effects for methyl transfer

AU - Wilson, Philippe B.

AU - Williams, Ian H.

PY - 2016/2/24

Y1 - 2016/2/24

N2 - 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.

AB - 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.

UR - http://dx.doi.org/10.1002/ange.201511708

UR - http://dx.doi.org/10.1002/ange.201511708

U2 - 10.1002/ange.201511708

DO - 10.1002/ange.201511708

M3 - Article

VL - 128

SP - 3244

EP - 3247

JO - Angewandte Chemie

JF - Angewandte Chemie

SN - 0044-8249

IS - 9

ER -