Cytochrome oxidase of an acidophilic iron-oxidizing bacterium, Thiobacillus ferrooxidans, functions at pH 3.5.
Cytochrome oxidase of Thiobacillus ferrooxidans was partially purified. The oxidase preparation had haems a and c, and oxidized ferrocytochrome c-552 of the bacterium. The optimal pH of the reaction was 3.5. The enzyme also oxidized the reduced form of rusticyanin, a copper protein of the bacterium. Our results indicate that the reduction of molecular oxygen by this enzyme may occur in the periplasm.
Kai
M
M
Department of Life Science, Faculty of Science, Tokyo Institute of Technology, Japan.
Yano
T
T
Fukumori
Y
Y
Yamanaka
T
T
D001400:Azurin / Q000031:analogs & derivatives / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000502:physiology*; D006418:Heme; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D013855:Thiobacillus / Q000201:enzymology* / Q000378:metabolism
D001426:Bacterial Proteins; D003574:Cytochrome c Group; C083951:cytochrome c553; C012543:rusticyanin; D001400:Azurin; D006418:Heme; C022302:cytochrome C-552; D003576:Electron Transport Complex IV