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

Halliwell, Tom, Fisher, Karl, Payne, Karl A. P., Rigby, Stephen E. J., Leys, David·2020·Microorganisms
DOI 10.3390/microorganisms8091344PMC PMC7565698
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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 Nitratireductor pacificus pht-3B catabolic 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 in crystallo 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.

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Metadata

Authors
Halliwell, T., Fisher, K., Payne, K. A. P., Rigby, S. E. J., & Leys, D.
Affiliations
Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK
ORCID
Venue
Microorganisms
Publisher
MDPI AG
Published
2020-09-02
Volume
8
Issue
9
Pages
1344
ISSN
2076-2607
DOI
10.3390/microorganisms8091344
PMC
PMC7565698
Cited by
18
References
0
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
Biotechnology and Biological Sciences Research Council (BB/M007316/1)

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