A methyl-CoM methylreductase system from methanogenic bacterium strain Gö 1 not requiring ATP for activity.
Crude inside-out vesicles from the methanogenic strain Gö1 were prepared via protoplasts. These vesicles catalyzed methane formation from methyl-CoM and H2 at a maximal rate of 35 nmol/min.mg protein. Methane formation by the vesicles did not depend on the addition of ATP. This was in contrast to conventionally prepared crude extracts from the same organism or from Methanosarcina barkeri which exhibited strict ATP dependence of methanogenesis. ATP analogues inhibited methanogenesis by extracts to a much higher extent than that by vesicles. Both, particulate and soluble components prepared from the crude vesicles by ultracentrifugation were necessary for ATP-independent methane formation from methyl-CoM and H2. Hydrogenase activity was mainly associated with the particulate fraction whereas methyl-CoM methylreductase could be assigned to the soluble fraction. The detergent sulfobetaine inhibited methane formation from methyl-CoM without affecting hydrogenase or titanium citrate-dependent methylreductase activities, indicating that an additional membraneous component is involved in methanogenesis for methyl-CoM and H2.
Deppenmeier
U
U
Institut für Mikrobiologie, Göttingen, FRG.
Blaut
M
M
Jussofie
A
A
Gottschalk
G
G
D000255:Adenosine Triphosphate / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D003593:Cytoplasm / Q000201:enzymology; D019605:Euryarchaeota / Q000201:enzymology*; D007700:Kinetics; D009097:Multienzyme Complexes / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*
D009097:Multienzyme Complexes; D000255:Adenosine Triphosphate; D010088:Oxidoreductases; C023895:methyl coenzyme M methylreductase