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Elucidation of the biosynthesis of the methane catalyst coenzyme F430.

Moore, S. and Sowa, S. and Schuchardt, C. and Deery, E. and Lawrence, A. and Ramos, J. and Billig, S. and Birkemeyer, C. and Chivers, P. and Howard, J. and Rigby, S. and Layer, G. and Warren, M. (2017) 'Elucidation of the biosynthesis of the methane catalyst coenzyme F430.', Nature., 543 (7643). pp. 78-82.


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
Full text:(AM) Accepted Manuscript
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Date accepted:25 January 2017
Date deposited:02 May 2017
Date of first online publication:22 February 2017
Date first made open access:22 August 2017

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