Is coenzyme M bound to factor F430 in methanogenic bacteria? Experiments with Methanobrevibacter ruminantium.
Coenzyme M (2-mercaptoethane sulfonic acid) and factor F430 (a nickel porphinoid) are coenzymes found in methanogenic bacteria. Recently it has been proposed that in these bacteria a coenzyme MF430 also exists which plays a key role in methane formation and in which coenzyme M and F430 are bound to each other. To test this hypothesis Methanobrevibacter ruminantium, which requires coenzyme M as a vitamin, was grown in the presence of [2-14C]CoMSH. F430 and 'CoM' (mixture of CoMSH and its disulfides) were quantitatively extracted from these cells and from partially purified methyl-CoM reductase using various methods. The extracts were chromatographed on cellulose or Sephadex G-10. Under all conditions factor F430 and 'CoM' were completely (greater than 99%) separated. There was no indication for the existence of a protein-free F430 species containing covalently bound coenzyme M in Mb. ruminantium. The results support the structure previously assigned to coenzyme F430.
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D019605:Euryarchaeota / Q000201:enzymology / Q000378:metabolism*; D008623:Mercaptoethanol / Q000031:analogs & derivatives*; D015080:Mesna / Q000302:isolation & purification / Q000378:metabolism*; D008665:Metalloporphyrins; D008667:Metalloproteins / Q000302:isolation & purification / Q000378:metabolism*; D009532:Nickel / Q000302:isolation & purification / Q000378:metabolism*; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature
D008665:Metalloporphyrins; D008667:Metalloproteins; D008623:Mercaptoethanol; C023540:factor F430; D009532:Nickel; D010088:Oxidoreductases; C021572:methyl coenzyme M reductase; D015080:Mesna