Journal of Biological Chemistry · 1980 · 72 citations · 5 references
Life SciencesBiochemistryMicrobiologyEnzymologyMicrobial MetabolismRedox BiochemistryCoenzyme ChemistryCofactor ChemistryEnzyme KineticsCofactor OrganizationCofactor SpecificityMethanogenesisMethanogenesis PathwaysOxidoreductase ActivityOxidoreductase CatalysisOxidoreductase Cofactors
A major simplification of the methyl coenzyme M methylreductase system of Methanobacterium has been effected. The 500,000-dalton hydrogenase complex has been replaced by an NADPH-coenzyme F420 oxidoreductase. By use of this electron-generating reaction, the methylreductase was found to be localized in component C, an acidic protein fraction. In the presence of the oxidoreductase and the methylreductase, formation of methane under a nitrogen atmosphere was dependent upon the addition of NADPH, coenzyme F420, component B (a new cofactor of unknown structure), ATP, Mg2+, and methyl coenzyme M.
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Structure and Methylation of Coenzyme M (HSCH2CH2SO3)
Craig D. Taylor, R. S. Wolfe · Journal of Biological Chemistry · 1974 · 256 citations · Full text
Pharmacy, Biochemistry, Chemistry +15