Journal
BIOCHEMISTRY-MOSCOW
Volume 68, Issue 11, Pages 1159-1170Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1023/B:BIRY.0000009129.18714.a4
Keywords
formate hydrogen lyase complex; formate dehydrogenase H; hydrogenase 3; hydrogenase 4; F0F1-ATPase; mixed-acid fermentation; Escherichia coli
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Formate hydrogen lyase from Escherichia coli is a membrane-bound complex that oxidizes formic acid to carbon dioxide and molecular hydrogen. Under anaerobic growth conditions and fermentation of sugars (glucose), it exists in two forms. One form is constituted by formate dehydrogenase H and hydrogenase 3, and the other one is the same formate dehydrogenase and hydrogenase 4; the presence of small protein subunits, carriers of electrons, is also probable. Other proteins may also be involved in formation of the enzyme complex, which requires the presence of metal (nickel-cobalt). Its formation also depends on the external pH and the presence of formate. Activity of both forms requires F0F1-ATPase; this explains dependence of the complex functioning on proton-motive force. It is also possible that the formate hydrogen lyase complex will exhibit its own proton-translocating function.
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