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. 1983 Apr;80(8):2151–2155. doi: 10.1073/pnas.80.8.2151

Component A of the methyl coenzyme M methylreductase system of Methanobacterium: resolution into four components.

D P Nagle Jr, R S Wolfe
PMCID: PMC393775  PMID: 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+.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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