FEBS Letters · 1986 · 35 citations · 18 references
Life SciencesBiochemistryMicrobiologyEnzymologyMetabolismMicrobial PhysiologyBacterial MetabolismCarbon FixationEnergy MetabolismMacromolecular AssemblyMembrane Protein Complex AnalysisMembrane Protein Complex AssemblyMembrane Protein SeparationMethanogenesisMethanogenesis PathwaysMethanotrophic BacteriaMethanotrophy
In Methanobacterium thermoautotrophicum , most of the sole cellular cobamide, 5‐hydroxybenzimidazolylcobamide (factor III [(1986) Anal. Biochem., submitted]) is bound to a membrane protein. This corrinoid protein is solubilized as a protein complex of M r ~500 000 by 5% nonpolar detergents. The complex is stable in 7 M urea. In SDS, two smaller fractions of M r ~ 30 000 and 60 000 carrying the cobamide are found. The unusual properties of the corrinoid enzyme complex suggest a novel function in the metabolism of CO 2 and Hz in methanogens.
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Methanogens: reevaluation of a unique biological group.
W E Balch, G. E. Fox, Linda J. Magrum et al. · Microbiological Reviews · 1979 · 1.5K citations
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