Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation

Karl A. P. Payne, Carolina P. Quezada, Karl Fisher, Mark S. Dunstan, Fraser A. Collins, Hanno Sjuts, Colin Levy, Sam Hay, Stephen E. J. Rigby and David Leys ()
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Karl A. P. Payne: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Carolina P. Quezada: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Karl Fisher: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Mark S. Dunstan: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Fraser A. Collins: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Hanno Sjuts: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Colin Levy: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Sam Hay: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
Stephen E. J. Rigby: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
David Leys: Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK

Nature, 2015, vol. 517, issue 7535, 513-516

Abstract: X-ray crystallography and EPR spectroscopy are used to characterize a soluble, oxygen-tolerant reductive dehalogenase from Nitratireductor pacificus pht-3B; the data suggest that the cobalt in the cobalamin cofactor ligates the halogen atom of the substrate, directly abstracting the halogen atom via an oxidative addition.

Date: 2015
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DOI: 10.1038/nature13901

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