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Is There a Dynamic Protein Contribution to the Substrate Trigger in Coenzyme B12-Dependent Ethanolamine Ammonia Lyase?

Authors

  • Dr. Alex R. Jones,

    Corresponding author
    1. Faculty of Life Sciences, Photon Science Institute and Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN (UK)
    • Faculty of Life Sciences, Photon Science Institute and Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN (UK)
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  • Dr. Samantha J. O. Hardman,

    1. Faculty of Life Sciences, Photon Science Institute and Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN (UK)
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  • Dr. Sam Hay,

    1. Faculty of Life Sciences, Photon Science Institute and Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN (UK)
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  • Prof. Nigel S. Scrutton

    Corresponding author
    1. Faculty of Life Sciences, Photon Science Institute and Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN (UK)
    • Faculty of Life Sciences, Photon Science Institute and Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN (UK)
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  • We thank the UK Biotechnology and Biological Sciences Research Council (BBSRC) and Electromagnetic Fields Biological Research Trust (EMF BRT) for funding. A.J. is a Colt Foundation Postdoctoral Research Fellow; S.H. is a BBSRC David Phillips Fellow; N.S. is a BBSRC Professorial Research Fellow and a Royal Society Wolfson Merit Award Holder. Thanks also go to Prof. Jonathan R. Woodward (University of Tokyo) for useful discussion regarding the spin chemistry and modelling.

Abstract

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Es ist bekannt, dass der Homolyse der Co-C-Bindung in Coenzym-B12-abhängiger Ethanolamin-Ammoniak-Lyase eine dissoziative Chemie folgt – aber wie steht es um die Beteiligung des Proteins? Experimente zeigen, dass die Reaktionsdynamik der Radikalpaarung an die schnelle Proteindynamik (ps–ns) der B12-Photolyse gekoppelt ist. Dies legt die Möglichkeit eines subtilen dynamischen Beitrags zur Homolyse nahe, der im Verbund mit der Elektrostatik und der H-Abstraktion vom Substrat agiert.

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