Elucidation of the biosynthesis of the methane catalyst coenzyme F430

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. Rigby, Gunhild Layer, Martin J. Warren

Research output: Contribution to journalArticlepeer-review

84 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)78-82
Number of pages5
Issue number7643
Early online date22 Feb 2017
Publication statusPublished - 2 Mar 2017

Cite this