Donor–Acceptor Distance Sampling Enhances the Performance of “Better than Nature” Nicotinamide Coenzyme Biomimetics.

Alexander Geddes, Caroline E. Paul, Sam Hay, Frank Hollmann, Nigel Scrutton

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Understanding the mechanisms of enzymatic
    hydride transfer with nicotinamide coenzyme
    biomimetics (NCBs) is critical to the enhanced performance
    of nicotinamide coenzyme dependent biocatalyts.
    Here the temperature dependence of kinetic isotope effects
    (KIEs) for hydride transfer between “Better than
    Nature” nicotinamide coenzyme biomimetics and several
    ene reductase (ER) biocatalysts is used to indicate
    transfer by quantum mechanical tunneling (QMT). A
    strong correlation between rate constants and the temperature
    dependence of the KIE (ΔΔH‡) for H/D transfer
    implies that faster reactions with NCBs are associated
    with enhanced donor-acceptor distance sampling. Our
    analysis provides the first mechanistic insight into how
    NCBs can outperform their natural counterparts and emphasizes
    the need to optimize donor-acceptor distance
    sampling to obtain high catalytic performance from Htransfer
    enzymes.
    Original languageEnglish
    JournalJournal of the American Chemical Society
    Volume138
    Issue number35
    Early online date23 Aug 2016
    DOIs
    Publication statusPublished - 2016

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