Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase

Henry J. Russell, Alex Jones, Sam Hay, Gregory M. Greetham, Michael Towrie, Nigel Scrutton

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture). © 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
    Original languageEnglish
    Pages (from-to)9306-9310
    Number of pages4
    JournalAngewandte Chemie International Edition
    Volume51
    Issue number37
    DOIs
    Publication statusPublished - 10 Sept 2012

    Keywords

    • enzymes
    • infrared spectroscopy
    • protein dynamics
    • reaction mechanism
    • ultrafast spectroscopy

    Research Beacons, Institutes and Platforms

    • Photon Science Institute

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