Reactivity of Desulfovibrio gigas hydrogenase toward artificial and natural electron donors or acceptors.
A purified preparation of hydrogenase from D. gigas was inactive toward ferredoxin, flavodoxin or rubredoxin in the absence of cytochrome c3 (M.W. 13,000), in an atmosphere of hydrogen, although direct reduction of benzyl viologen or FMN was possible. The hydrogen evolution reaction from dithionite was possible with methyl viologen. The same reaction also occured with cytochrome c3 (M.W. 13,000) or cytochrome c3 (M.W. 26,000). Addition of either ferredoxin or flavodoxin did not accelerate the reaction.
D003901:Desulfovibrio / Q000201:enzymology*; D004579:Electron Transport; D006859:Hydrogen; D008970:Molecular Weight; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D006859:Hydrogen; D010088:Oxidoreductases