Moore, Simon (2017) Elucidation of the biosynthesis of the methane catalyst coenzyme F430. Nature, 543 . pp. 78-82. ISSN 0028-0836. E-ISSN 1476-4687. (KAR id:85694)
PDF
Author's Accepted Manuscript
Language: English |
|
Download this file (PDF/1MB) |
Preview |
Request a format suitable for use with assistive technology e.g. a screenreader | |
XML Word Processing Document (DOCX)
Author's Accepted Manuscript
Language: English Restricted to Repository staff only |
|
Contact us about this Publication
|
|
PDF
Publisher pdf
Language: English |
|
Download this file (PDF/4MB) |
Preview |
Request a format suitable for use with assistive technology e.g. a screenreader |
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.
Item Type: | Article |
---|---|
Subjects: |
Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology (Living systems) > QP517 Biochemistry |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Simon Moore |
Date Deposited: | 27 Jan 2021 12:34 UTC |
Last Modified: | 16 Feb 2021 14:17 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/85694 (The current URI for this page, for reference purposes) |
- Link to SensusAccess
- Export to:
- RefWorks
- EPrints3 XML
- BibTeX
- CSV
- Depositors only (login required):