Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope.

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ID: 118516
2020
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Abstract
Reductive dehalogenases are responsible for the reductive cleavage of carbon-halogen bonds during organohalide respiration. A variety of mechanisms have been proposed for these cobalamin and [4Fe-4S] containing enzymes, including organocobalt, radical, or cobalt-halide adduct based catalysis. The latter was proposed for the oxygen-tolerant cataboli reductive dehalogenase (NpRdhA). Here, we present the first substrate bound NpRdhA crystal structures, confirming a direct cobalt-halogen interaction is established and providing a rationale for substrate preference. Product formation is observed due to X-ray photoreduction. Protein engineering enables rational alteration of substrate preference, providing a future blue print for the application of this and related enzymes in bioremediation.
Reference Key
halliwell2020catabolicmicroorganisms Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Halliwell, Tom;Fisher, Karl;Payne, Karl A P;Rigby, Stephen E J;Leys, David;
Journal Microorganisms
Year 2020
DOI
E1344
URL
Keywords
X-ray crystallography bioremediation epr cobalamin iron-sulphur clusters reductive dehalogenase

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