ATP activation and properties of the methyl coenzyme M reductase system in Methanobacterium thermoautotrophicum.
The requirement of ATP for the methyl coenzyme M methylreductase in extracts of Methanobacterium thermoautotrophicum was found to be catalytic; for each mol of ATP added, 15 mol of methane was produced from methyl coenzyme M [2-(methylthio)ethanesulfonic acid]. Other nucleotide triphosphates partially replaced ATP in activation of the reductase. All components of the reaction were found in the supernatant fraction of cell extracts after centrifugation at 100,000 X g for 1 h; optimal reaction rates occurred at 65 degrees C, at a pH range of 5.6 to 6.0, and at concentrations of ATP and MgCl2 of 1 mM and 40 mM, respectively. Chloral hydrate, chloroform, nitrite, 2,4-dinitrophenol, and viologen dyes (compounds known to inhibit methanogenesis from a variety of substrates) were found to inhibit the conversion of methyl coenzyme M to methane. Methyl coenzyme M methylreductase was shown to be present in a variety of methanogens.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D004789:Enzyme Activation; D019605:Euryarchaeota / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D015080:Mesna; D008697:Methane / Q000096:biosynthesis; D009711:Nucleotides / Q000494:pharmacology; D010088:Oxidoreductases / Q000378:metabolism*; D013696:Temperature
D009711:Nucleotides; D000255:Adenosine Triphosphate; D010088:Oxidoreductases; C021572:methyl coenzyme M reductase; D008274:Magnesium; D015080:Mesna; D008697:Methane