The terminal oxidase of Photobacterium phosphoreum. A novel cytochrome.
The terminal oxidase of Photobacterium phosphoreum has been purified to the electrophoretically homogeneous state and some of its properties have been studied. The enzyme catalyses oxidation of ascorbate in the presence of phenazine methosulphate or N,N,N',N'-tetramethyl-p-phenylenediamine. The reaction is inhibited by cyanide. Nitrite at comparatively high concentrations inhibits the enzyme, but the enzyme does not catalyse nitrite reduction with ascorbate plus the electron mediator as the electron donor. The enzyme shows the absorption peaks at 632, 565, 534 and 436 nm in the reduced form. It has two kinds of haems: protohaem and haem d. Namely, the enzyme is a 'cytochrome bd'-type oxidase; a novel cytochrome.
D003580:Cytochromes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010101:Oxygen Consumption; D010776:Photobacterium / Q000201:enzymology*; D013053:Spectrophotometry
D003580:Cytochromes; D010088:Oxidoreductases