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

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 la...

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Bibliographic Details
Published in:Microorganisms (Basel) 2020-09, Vol.8 (9), p.1344
Main Authors: Halliwell, Tom, Fisher, Karl, Payne, Karl A P, Rigby, Stephen E J, Leys, David
Format: Article
Language:English
Subjects:
Bioremediation
Catalysis
cobalamin
Cobalt
Crystal structure
E coli
Enzymes
EPR
Iron
iron-sulphur clusters
Ligands
Phenols
Photoreduction
Protein engineering
Proteins
reductive dehalogenase
Respiration
Spectrum analysis
Substrate preferences
Substrates
Vitamin B12
X-ray crystallography
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Summary: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.
ISSN:2076-2607
2076-2607
DOI:10.3390/microorganisms8091344