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Elucidation of the biosynthesis of the methane catalyst coenzyme F430

Moore, Simon J., Sowa, Sven T., Schuchardt, Christopher, Deery, Evelyne, Lawrence, Andrew D., Ramos, José Vazquez, Billig, Susan, Birkemeyer, Claudia, Chivers, Peter T., Howard, Mark J., and others. (2017) Elucidation of the biosynthesis of the methane catalyst coenzyme F430. Nature, (543). pp. 78-82. ISSN 0028-0836. E-ISSN 1476-4687. (doi:10.1038/nature21427) (KAR id:60555)

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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.

Item Type: Article
DOI/Identification number: 10.1038/nature21427
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 27 Feb 2017 10:59 UTC
Last Modified: 23 Jan 2020 04:13 UTC
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Moore, Simon J.:
Warren, Martin J.:
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