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

Sam Hay, Christopher Pudney, Parvinder Hothi, Linus O Johannissen, Laura Masgrau, Jiayun Pang, David Leys, Michael J Sutcliffe, Nigel S Scrutton

Research output: Contribution to journalArticle

18 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)16-21
JournalBiochemical Society Transactions
Volume36
DOIs
Publication statusPublished - 2008

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