Properties of ubiquinol oxidase reconstituted from ubiquinol-cytochrome c reductase, cytochrome c and cytochrome c oxidase
نویسندگان
چکیده
منابع مشابه
Cytochrome c-mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool.
Ubiquinol oxidase has been reconstituted from ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase (Complex IV). The steady-state level of reduction of cytochrome c by ubiquinol-2 varies with the molar ratios of the complexes and with the presence of antimycin in a way that can be quantitatively accounted for by a model in which cytochrome c acts as a freely dif...
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A purified, active succinate-ubiquinone reductase was prepared from succinate-cytochrome c reductase without damage to ubiquinol-cytochrome c reductase by 1.1% Triton X-100 solubilization at pH 8.0, and calcium phosphate column chromatography in 50 mM Tris-succinate buffer, pH 8.0, containing 30 mM potassium phosphate. Succinate-ubiquinone reductase thus obtained contains ubiquinone and catalyz...
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Cytochrome c oxidase is an intricate metalloprotein that transfers electrons from cytochrome c to oxygen in the last step of the mitochondrial respiratory chain. It uses the free energy of this reaction to sustain a transmembrane electrochemical gradient of protons. Site-directed mutagenesis studies of bacterial terminal oxidases and the recent availability of refined crystal structures of the ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1982
ISSN: 0306-3283
DOI: 10.1042/bj2020527