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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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“Cohort-ry” in motion: The chemistry following Co[BOND]C bond homolysis in coenzyme B12-dependent ethanolamine ammonia lyase is known to favor dissociation, but what of the protein contribution? Experiments reveal the radical pair reaction dynamics to be coupled to the ps–ns protein dynamics in B12 photolysis. This raises the possibility of a subtle, dynamic contribution to homolysis, which acts in cohort with electrostatics and H-abstraction from the substrate.

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