Reductive activation of the methyl coenzyme M methylreductase system of Methanobacterium thermoautotrophicum delta H

Journal Article · Thu Sep 01 00:00:00 EDT 1988 · J. Bacteriol.; (United States)

OSTI ID:6829518

Rouviere, P E; Bobik, T A; Wolfe, R S

When titanium(III) citrate was used as electron donor for the reduction of methyl coenzyme M by the methyl coenzyme M methylreductase system of Methanobacterium thermoautotrophicum delta H, component A1 was no longer required. The simpler system thus obtained required components A2, A3, and C as well as catalytic amounts of ATP, vitamin B-12, and the disulfide of 7-mercaptoheptanoylthreonine phosphate in addition to titanium(III) citrate. This three component enzyme system also could produce CH/sub 4/ when stoichiometric amounts of 7-mercaptoheptanoylthreonine phosphate were used as a source of electrons under an H/sub 2/ atmosphere. When 7-mercaptoheptanoylthreonine phosphate or H/sub 2/ was used alone no CH/sub 4/ was produced, indicating a dual requirement for reducing equivalents: one to activate the methylreductase system and the other to reduce methyl coenzyme M. This is the first evidence that the activation of methyl coenzyme M methylreductase is a reductive process.

• Research Organization: Univ. of Illinois, Urbana (USA)
• OSTI ID: 6829518
• Journal Information: J. Bacteriol.; (United States), Journal Name: J. Bacteriol.; (United States) Vol. 170:9; ISSN JOBAA
• Country of Publication: United States
• Language: English

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ALKANES
BACTERIA
BIOSYNTHESIS
CARBOXYLIC ACID SALTS
CHEMICAL REACTIONS
CITRATES
ELECTRONS
ELEMENTARY PARTICLES
ENZYME ACTIVITY
ENZYMES
FERMIONS
GROWTH
HYDROCARBONS
LEPTONS
METHANE
METHANOGENIC BACTERIA
MICROORGANISMS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
REDOX REACTIONS
SYNTHESIS
TITANIUM COMPOUNDS
TRANSITION ELEMENT COMPOUNDS