Reconstitution of bovine cytochrome c oxidase.
نویسندگان
چکیده
منابع مشابه
Redox-Controlled Proton Gating in Bovine Cytochrome c Oxidase
Cytochrome c oxidase is the terminal enzyme in the electron transfer chain of essentially all organisms that utilize oxygen to generate energy. It reduces oxygen to water and harnesses the energy to pump protons across the mitochondrial membrane in eukaryotes and the plasma membrane in prokaryotes. The mechanism by which proton pumping is coupled to the oxygen reduction reaction remains unresol...
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Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-coupled transmembrane proton pump, which i...
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In the preceding paper the oxidation of substrates by “indophenol oxidase” was demonstrated to be a joint action of cytochrome and cytochrome oxidase. It was further shown that with a given amount of oxidase the velocity of hydroquinone oxidation reached a maximum as the amount of added cytochrome was increased. The latter fact immediately suggested the probability that the rapid aerobic oxidat...
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Copper can be removed from bovine cytochrome c oxidase with bathocuproine disulfonate under anaerobic conditions in the presence of reduced cytochrome c. The copper-depleted enzyme is relatively inactive. Upon replacement of copper with Cu’-acetonitrile, more than the original activity is regained. The rate of O2 consumption catalyzed by the reconstituted enzyme is unaffected by catalase; the p...
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Mitochondrial cytochrome c oxidase utilizes electrons provided by cytochrome c for the active vectorial transport of protons across the inner mitochondrial membrane through the reduction of molecular oxygen to water. Direct structural evidence on the transient cytochrome c oxidase-cytochrome c complex thus far, however, remains elusive and its physiological relevant oligomeric form is unclear. ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1999
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.39.s121_2