A cytochrome o-type oxidase of the thermophilic bacterium PS3 grown under air-limited conditions.
A cytochrome o-type oxidase from the thermophilic bacterium PS3 grown under air-limited conditions was purified by ion-exchange chromatography in the presence of a non-ionic detergent. The enzyme was composed of three subunits (60, 30, and 16 kDa) and seemed to contain two molecules of heme b as prosthetic groups. It contained no detectable copper. The reduced enzyme showed absorption bands at 426 and 558.5 nm, and a characteristic spectral change upon binding CO. It oxidized several cytochromes c and artificial dyes such as N,N,N',N'-tetramethyl-p-phenylenediamine and phenazonium methosulfate at appreciable rates. Its Km for O2 was low (0.09 microM). It was capable of transmembrane electron transfer, because when reconstituted into liposomes, it generated a membrane potential upon oxidation without pumping protons.
Sone
N
N
Department of Biochemistry, Jichi Medical School, Tochigi.
Kutoh
E
E
Sato
K
K
D001273:Atmosphere Exposure Chambers; D001406:Bacillaceae / Q000201:enzymology* / Q000254:growth & development; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013053:Spectrophotometry
C038862:cytochrome o oxidase; D003576:Electron Transport Complex IV