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Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer

Kunze, Cindy, Bommer, Martin, Hagen, Wilfred R., Uksa, Marie, Dobbek, Holger, Schubert, Torsten, Diekert, Gabriele·2017·Nature Communications
DOI 10.1038/ncomms15858PMC PMC5500849
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Abstract

The capacity of metal-containing porphyrinoids to mediate reductive dehalogenation is implemented in cobamide-containing reductive dehalogenases (RDases), which serve as terminal reductases in organohalide-respiring microbes. RDases allow for the exploitation of halogenated compounds as electron acceptors. Their reaction mechanism is under debate. Here we report on substrate–enzyme interactions in a tetrachloroethene RDase (PceA) that also converts aryl halides. The shape of PceA’s highly apolar active site directs binding of bromophenols at some distance from the cobalt and with the hydroxyl substituent towards the metal. A close cobalt–substrate interaction is not observed by electron paramagnetic resonance spectroscopy. Nonetheless, a halogen substituent para to the hydroxyl group is reductively eliminated and the path of the leaving halide is traced in the structure. Based on these findings, an enzymatic mechanism relying on a long-range electron transfer is concluded, which is without parallel in vitamin B 12 -dependent biochemistry and represents an effective mode of RDase catalysis.

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Metadata

Authors
Kunze, C., Bommer, M., Hagen, W. R., Uksa, M., Dobbek, H., Schubert, T., & Diekert, G.
ORCID
Schubert, Torsten
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2017-07-03
Volume
8
Issue
1
ISSN
2041-1723
DOI
10.1038/ncomms15858
PMC
PMC5500849
Cited by
104
References
1
Language
en
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