Atomistic insight into the origin of the temperature-dependence of kinetic isotope effects and H-tunnelling in enzyme systems is revealed through combined experimental studies and biomolecular simulation.

Biochemical Society Transactions
Sam HayN S Scrutton

Abstract

The physical basis of the catalytic power of enzymes remains contentious despite sustained and intensive research efforts. Knowledge of enzyme catalysis is predominantly descriptive, gained from traditional protein crystallography and solution studies. Our goal is to understand catalysis by developing a complete and quantitative picture of catalytic processes, incorporating dynamic aspects and the role of quantum tunnelling. Embracing ideas that we have spearheaded from our work on quantum mechanical tunnelling effects linked to protein dynamics for H-transfer reactions, we review our recent progress in mapping macroscopic kinetic descriptors to an atomistic understanding of dynamics linked to biological H-tunnelling reactions.

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Citations

Sep 4, 2008·Photosynthesis Research·Sam Hay, Nigel S Scrutton
Apr 9, 2009·Journal of the American Chemical Society·Michelle K LudlowSharon Hammes-Schiffer
Dec 3, 2014·Proceedings of the National Academy of Sciences of the United States of America·C Tony LiuStephen J Benkovic
Apr 4, 2015·Physical Chemistry Chemical Physics : PCCP·Linus O JohannissenNigel S Scrutton
Jul 10, 2008·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Sam HayNigel S Scrutton
Jan 16, 2009·Angewandte Chemie·Sam HayNigel S Scrutton
Mar 17, 2016·Journal of Sex Research·L Monique Ward
Mar 18, 2009·Biochemical Society Transactions·Andrew W Munro, Nigel S Scrutton
Feb 23, 2012·Nature Chemistry·Sam Hay, Nigel S Scrutton
Nov 7, 2009·Journal of the American Chemical Society·Christopher R PudneyNigel S Scrutton
Feb 5, 2013·Journal of the American Chemical Society·Christopher R PudneyNigel S Scrutton

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