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

Author

Listed:
  • Cindy Kunze

    (Institute of Microbiology, Friedrich Schiller University)

  • Martin Bommer

    (Structural Biology/Biochemistry, Institute of Biology, Humboldt Universität zu Berlin
    Present address: Max-Delbrück-Centrum for Molecular Medicine, Robert-Roessle-Str. 10, Berlin D-13092, Germany)

  • Wilfred R. Hagen

    (Faculty of Applied Sciences, Delft University of Technology)

  • Marie Uksa

    (Institute of Microbiology, Friedrich Schiller University
    Present address: Institute of Soil Science and Land Evaluation, University of Hohenheim, Emil-Wolff-Strasse 27, Stuttgart D-70593, Germany)

  • Holger Dobbek

    (Structural Biology/Biochemistry, Institute of Biology, Humboldt Universität zu Berlin)

  • Torsten Schubert

    (Institute of Microbiology, Friedrich Schiller University)

  • Gabriele Diekert

    (Institute of Microbiology, Friedrich Schiller University)

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 B12-dependent biochemistry and represents an effective mode of RDase catalysis.

Suggested Citation

  • Cindy Kunze & Martin Bommer & Wilfred R. Hagen & Marie Uksa & Holger Dobbek & Torsten Schubert & Gabriele Diekert, 2017. "Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer," Nature Communications, Nature, vol. 8(1), pages 1-11, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15858
    DOI: 10.1038/ncomms15858
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    Cited by:

    1. Lorenzo Cimmino & Américo G. Duarte & Dongchun Ni & Babatunde E. Ekundayo & Inês A. C. Pereira & Henning Stahlberg & Christof Holliger & Julien Maillard, 2023. "Structure of a membrane-bound menaquinol:organohalide oxidoreductase," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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