| Literature DB >> 6403944 |
Abstract
Component A, the oxygen-sensitive protein fraction of the methyl coenzyme M methylreductase system of Methanobacterium thermoautotrophicum, has been stabilized and resolved into three protein fractions and one cofactor that are required to reconstitute component A activity. Component A1 is oxygen-stable and contains hydrogen-dependent deazaflavin (coenzyme F420)-reducing activity. Component A2 is acidic; components A2 and A3 are oxygen sensitive. The specific functions of each component in methyl group reduction are unknown. Resolution of component A revealed a new cofactor requirement of the methylreductase system for FAD. Hydrogen-dependent reduction of methyl coenzyme M to methane and coenzyme M, the terminal step of CO2 reduction by methanogenic bacteria, requires protein components A1, A2, A3, and C in addition to component B, FAD, ATP, and Mg2+.Entities:
Mesh:
Substances:
Year: 1983 PMID: 6403944 PMCID: PMC393775 DOI: 10.1073/pnas.80.8.2151
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205