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Elucidation of the biosynthesis of the methane catalyst coenzyme F430

Moore, S.; Sowa, S.; Schuchardt, C.; Deery, E.; Lawrence, A.; Ramos, J.; Billig, S.; Birkemeyer, C.; Chivers, P.; Howard, J.; Rigby, S.; Layer, G.; Warren, M.

Elucidation of the biosynthesis of the methane catalyst coenzyme F430 Thumbnail


Authors

S. Moore

S. Sowa

C. Schuchardt

E. Deery

A. Lawrence

J. Ramos

S. Billig

C. Birkemeyer

J. Howard

S. Rigby

G. Layer

M. Warren



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.

Journal Article Type Article
Acceptance Date Jan 25, 2017
Online Publication Date Feb 22, 2017
Publication Date Feb 22, 2017
Deposit Date Apr 6, 2017
Publicly Available Date Aug 22, 2017
Journal Nature
Print ISSN 0028-0836
Electronic ISSN 1476-4687
Publisher Nature Research
Peer Reviewed Peer Reviewed
Volume 543
Issue 7643
Pages 78-82
DOI https://doi.org/10.1038/nature21427
Public URL https://durham-repository.worktribe.com/output/1389542

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