Elucidation of the biosynthesis of the methane catalyst coenzyme F 430

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 F , a nickel-containing modified tetrapyrrole that promotes catalys...

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Bibliographic Details
Published in:Nature (London) 2017-03, Vol.543 (7643), p.78
Main Authors: 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, Rigby, Stephen E J, Layer, Gunhild, Warren, Martin J
Format: Article
Language:English
Subjects:
Amidohydrolases - genetics
Amidohydrolases - metabolism
Biocatalysis
Biosynthetic Pathways - genetics
Coenzymes - biosynthesis
Coenzymes - chemistry
Lyases - genetics
Lyases - metabolism
Metalloporphyrins - chemistry
Metalloporphyrins - metabolism
Methane - analogs & derivatives
Methane - biosynthesis
Methane - metabolism
Methanosarcina barkeri - enzymology
Methanosarcina barkeri - genetics
Methanosarcina barkeri - metabolism
Multigene Family
Nickel - metabolism
Oxidoreductases - genetics
Oxidoreductases - metabolism
Tetrapyrroles - biosynthesis
Tetrapyrroles - chemistry
Uroporphyrins - chemistry
Uroporphyrins - metabolism
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Summary: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 F , a nickel-containing modified tetrapyrrole that promotes catalysis through a methyl radical/Ni(ii)-thiolate intermediate. However, it is unclear how coenzyme F 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 F 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.
ISSN:1476-4687
DOI:10.1038/nature21427