Barrier compression enhances an enzymatic hydrogen-transfer reaction

Sam Hay, Christopher R. Pudney, Tom A. McGrory, Jiayun Pang, Michael J. Sutcliffe, Nigel S. Scrutton

    Research output: Contribution to journalArticlepeer-review


    Putting the squeeze on: Hydrostatic pressure causes a shortening of the charge-transfer bond in the binary complex of morphinone reductase and NADH 4 (see diagram). Molecular dynamics simulations suggest that pressure reduces the average reaction barrier width by restricting the conformational space available to the flavin mononucleotide and NADH within the active site. The apparent rate of catalysis increases with pressure. © 2009 Wiley-VCH Verlag GmbH amp; Co. KGaA.
    Original languageEnglish
    Pages (from-to)1452-1454
    Number of pages2
    JournalAngewandte Chemie - International Edition
    Issue number8
    Publication statusPublished - 9 Feb 2009


    • Enzyme catalysis
    • Hydrogen transfer
    • Molecular dynamics
    • Quantum chemistry
    • Reaction barrier


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