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Title: Carbon monoxide-dependent methyl coenzyme M methylreductase in acetotrophic Methosarcina spp

Journal Article · · J. Bacteriol.; (United States)
OSTI ID:6384429

Cell extracts of acetate-grown Methanosarcina strain TM-1 and Methanosarcina acetivorans both contained CH/sub 3/-S-CoM methylreductase activity. The methylreductase activity was supported by CO and H/sub 2/ but not by formate as electron donors. The CO-dependent activity was equivalent to the H/sub 2/-dependent activity in strain TM-1 and was fivefold higher than the H/sub 2/-dependent activity of M. acetivorans. When strain TM-1 was cultured on methanol, the CO-dependent activity was reduced to 5% of the activity in acetate-grown cells. Methanobacterium formicicum grown on H/sub 2/-CO/sub 2/ contained no CO-dependent methylreductase activity. The CO-dependent methylreductase of strain TM-1 had a pH optimum of 5.5 and a temperature optimum of 60/sup 0/C. The activity was stimulated by the addition of MgCl/sub 2/ and ATP. Both acetate-grown strain TM-1 and acetate-grown M. acetivorans contained CO dehydrogenase activities of 9.1 and 3.8 U/mg, respectively, when assayed with methyl viologen. The CO dehydrogenase of acetate-grown cells rapidly reduced FMN and FAD, but coenzyme F/sub 420/ and NADP/sup +/ were poor electron acceptors. No formate dehydrogenase was detected in either organism when grown on acetate. The results suggest that a CO-dependent CH/sub 3/-S-CoM methylreductase system is involved in the pathway of the conversion of acetate to methane and that free formate is not an intermediate in the pathway.

Research Organization:
Virginia Polytechnic Inst. and State Univ., Blacksburg
OSTI ID:
6384429
Journal Information:
J. Bacteriol.; (United States), Vol. 160:2
Country of Publication:
United States
Language:
English