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The octahaem MccA is a haem c–copper sulfite reductase

Author

Listed:
  • Bianca Hermann

    (Lehrstuhl Biochemie, Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany)

  • Melanie Kern

    (Microbial Energy Conversion & Biotechnology, Technische Universität Darmstadt, Schnittspahnstrasse 10, 64287 Darmstadt, Germany)

  • Luigi La Pietra

    (Microbial Energy Conversion & Biotechnology, Technische Universität Darmstadt, Schnittspahnstrasse 10, 64287 Darmstadt, Germany)

  • Jörg Simon

    (Microbial Energy Conversion & Biotechnology, Technische Universität Darmstadt, Schnittspahnstrasse 10, 64287 Darmstadt, Germany)

  • Oliver Einsle

    (Lehrstuhl Biochemie, Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany
    BIOSS Centre for Biological Signalling Studies, Schänzlestrasse 1, 79104 Freiburg, Germany)

Abstract

Sulfite-reducing microbes couple the reduction of sulfite to the generation of a proton motive force that sustains organismic growth; here, two X-ray crystal structures are solved of MccA, a c-type cytochrome enzyme with eight haem groups that catalyses the six-electron reduction of sulfite to sulfide at a novel haem–copper active site.

Suggested Citation

  • Bianca Hermann & Melanie Kern & Luigi La Pietra & Jörg Simon & Oliver Einsle, 2015. "The octahaem MccA is a haem c–copper sulfite reductase," Nature, Nature, vol. 520(7549), pages 706-709, April.
    • Handle: RePEc:nat:nature:v:520:y:2015:i:7549:d:10.1038_nature14109
    DOI: 10.1038/nature14109
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    Cited by:

    1. Jiao Li & Wan Zheng & Ming Gu & Long Han & Yanmei Luo & Koukou Yu & Mengxin Sun & Yuliang Zong & Xiuxiu Ma & Bing Liu & Ethan P. Lowder & Deanna L. Mendez & Robert G. Kranz & Kai Zhang & Jiapeng Zhu, 2022. "Structures of the CcmABCD heme release complex at multiple states," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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