Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the "strict anaerobe" Desulfovibrio gigas.
A rubredoxin-oxygen oxidoreductase, a homodimer with a molecular weight of 43 kDa per monomer, was found to be a component of an electron transfer chain that couples the reduction of oxygen to water with NADH oxidation. This FAD-containing protein appears to contain a new type of heme group. The electron transfer chain is not inhibited by cyanide and azide. In contrast, CO decreases NADH oxidation rate and also induces release of the prosthetic groups from the native terminal reductase.
Department of Biochemistry, University of Georgia, Athens 30602.
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L
Chen
M Y
MY
Liu
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J
LeGall
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Fareleira
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Santos
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AV
Xavier
D002850:Chromatography, Gel; D002854:Chromatography, Paper; D003901:Desulfovibrio / Q000201:enzymology / Q000378:metabolism*; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D014867:Water / Q000378:metabolism*
D014867:Water; D009243:NAD; D010088:Oxidoreductases; C081469:rubredoxin-oxygen oxidoreductase; D010100:Oxygen