Enzymological studies of one-carbon reactions in the pathway of acetate utilization by methanogenic bacteria: Annual technical report for the period 6/1/87 to 1/31/88

Technical Report · Fri Jan 01 04:00:00 EST 1988

OSTI ID:5429132

Ferry, J G

The general pathway of acetate conversion to methane in Methanosarcina thermophila is known and several of the enzymes have been characterized. AcetylCoA is cleaved by a enzyme complex with carbon monoxide dehydrogenases activity. The methyl group is transferred to Coenzyme M and the carbonyl to the nickel site in the complex. Methylcoenzyme M is reductively demethylated to methane with electrons derived from the oxidation of the bound carbonyl. A ferredoxin is the immediate electron acceptor of electrons leaving the complex. Membrane components are implicated in electron transport from the ferredoxin to methylcoenzyme m. A corrinoid protein in the complex is thought to catalyze methyl transfer, electron transfer, or both. All of the above proteins have been purified except the corrinoid protein. Our laboratory is investigating the catalytic mechanism of the purified proteins. Biochemical characterizations of all proteins will include amino acid analysis and N-terminal sequencing, kinetic parameters, physical and other properties. 2 tabs.

• Research Organization: Virginia Polytechnic Inst., Blacksburg (USA)
• DOE Contract Number: FG05-87ER13730
• OSTI ID: 5429132
• Report Number(s): DOE/ER/13730-1; ON: DE88006539
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
ACETATES
ALKANES
BACTERIA
BIOSYNTHESIS
CARBON COMPOUNDS
CARBON MONOXIDE
CARBON OXIDES
CARBOXYLIC ACID SALTS
CATABOLISM
CHALCOGENIDES
CYTOCHROMES
DOCUMENT TYPES
ENZYME ACTIVITY
ENZYMES
FERREDOXIN
FRACTIONATION
HYDROCARBONS
METABOLISM
METALLOPROTEINS
METHANE
METHANOGENIC BACTERIA
MICROORGANISMS
ORGANIC COMPOUNDS
OXIDES
OXIDOREDUCTASES
OXYGEN COMPOUNDS
PIGMENTS
PROGRESS REPORT
PROTEINS
SEPARATION PROCESSES
SYNTHESIS