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Elucidation of the biosynthesis of the methane catalyst coenzyme F430

Author

Listed:
  • Simon J. Moore

    (School of Biosciences, University of Kent, Giles Lane)

  • Sven T. Sowa

    (Institute of Biochemistry, Leipzig University, Brüderstrasse 34, 04103 Leipzig, Germany)

  • Christopher Schuchardt

    (Institute of Biochemistry, Leipzig University, Brüderstrasse 34, 04103 Leipzig, Germany)

  • Evelyne Deery

    (School of Biosciences, University of Kent, Giles Lane)

  • Andrew D. Lawrence

    (School of Biosciences, University of Kent, Giles Lane)

  • José Vazquez Ramos

    (Institute of Biochemistry, Leipzig University, Brüderstrasse 34, 04103 Leipzig, Germany)

  • Susan Billig

    (Institute of Analytical Chemistry, Leipzig University, Linnéstrasse 3, 04103 Leipzig, Germany)

  • Claudia Birkemeyer

    (Institute of Analytical Chemistry, Leipzig University, Linnéstrasse 3, 04103 Leipzig, Germany)

  • Peter T. Chivers

    (Durham University)

  • Mark J. Howard

    (School of Biosciences, University of Kent, Giles Lane)

  • Stephen E. J. Rigby

    (Manchester Institute of Biotechnology, School of Chemistry, University of Manchester)

  • Gunhild Layer

    (Institute of Biochemistry, Leipzig University, Brüderstrasse 34, 04103 Leipzig, Germany)

  • Martin J. Warren

    (School of Biosciences, University of Kent, Giles Lane)

Abstract

Methane biogenesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible for the utilization of methane through anaerobic methane oxidation. The enzyme uses an ancillary factor called coenzyme F430, a nickel-containing modified tetrapyrrole that promotes catalysis through a methyl radical/Ni(ii)-thiolate intermediate. However, it is unclear how coenzyme F430 is synthesized from the common primogenitor uroporphyrinogen iii, incorporating 11 steric centres into the macrocycle, although the pathway must involve chelation, amidation, macrocyclic ring reduction, lactamization and carbocyclic ring formation. Here we identify the proteins that catalyse the biosynthesis of coenzyme F430 from sirohydrochlorin, termed CfbA–CfbE, and demonstrate their activity. The research completes our understanding of how the repertoire of tetrapyrrole-based pigments are constructed, permitting the development of recombinant systems to use these metalloprosthetic groups more widely.

Suggested Citation

  • Simon J. Moore & Sven T. Sowa & Christopher Schuchardt & Evelyne Deery & Andrew D. Lawrence & José Vazquez Ramos & Susan Billig & Claudia Birkemeyer & Peter T. Chivers & Mark J. Howard & Stephen E. J., 2017. "Elucidation of the biosynthesis of the methane catalyst coenzyme F430," Nature, Nature, vol. 543(7643), pages 78-82, March.
    • Handle: RePEc:nat:nature:v:543:y:2017:i:7643:d:10.1038_nature21427
    DOI: 10.1038/nature21427
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