Methane formation from methyl-coenzyme M in a system containing methyl-coenzyme M reductase, component B and reduced cobalamin.
Purified methyl-CoM reductase of Methanobacterium thermoautotrophicum was found to catalyze the reduction of methyl-coenzyme M to methane at a specific rate of 100 nmol X min-1 X mg protein-1 in a system containing partially purified component B, cob(III)alamin (B-12a), and, as electron donors, dithiothreitol or SnCl2. Under these experimental conditions B-12a was reduced to cob(II)alamin (B-12r), which is known to disproportionate to cob(I)alamin (B-12s) and B-12a to a slight extent. Methane formation from methyl-CoM was inhibited by propyl iodide, methyl iodide, chloroform and carbon tetrachloride, which were shown to react with B-12s to the corresponding light-sensitive alkyl cobalamin. Inhibition by propyl iodide was less effective in light-exposed samples. From these findings it is concluded that in this assay system B-12s might serve as electron donor for the enzymatic reduction of methyl-CoM to methane.
Ankel-Fuchs
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D
Thauer
R K
RK
D002384:Catalysis; D004229:Dithiothreitol / Q000378:metabolism; D019605:Euryarchaeota / Q000201:enzymology; D008623:Mercaptoethanol / Q000031:analogs & derivatives*; D015080:Mesna / Q000031:analogs & derivatives* / Q000302:isolation & purification / Q000378:metabolism; D008697:Methane / Q000096:biosynthesis*; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D014805:Vitamin B 12 / Q000378:metabolism*
C023349:methyl coenzyme M; D008623:Mercaptoethanol; D010088:Oxidoreductases; C021572:methyl coenzyme M reductase; D015080:Mesna; D008697:Methane; D014805:Vitamin B 12; D004229:Dithiothreitol