A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.
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چکیده
منابع مشابه
A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.
Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC 1.9.3.1) was purified from the cytoplasmic membrane of the bacterium Paracoccus denitrificans. The enzyme contains two heme groups (a and a3) and two copper atoms per minimal unit, oxidizes mammalian cytochrome c at a high rate, and, when incorporated into liposomes, generates an electrochemical proton gradient during cytochrome...
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Cytochrome c oxidase purified from the bacterium Paracoccus denitrificans was analyzed by analytical ultracentrifugation. In the detergent octyltetra/pentaoxyethylene (C8E45), the isolated enzyme exhibits a molecular weight of 79,000 to 84,000. The detergent-solubilized enzyme is thus a monomer which contains one copy of each of the two subunits.
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The heme aa3 type cytochrome oxidase from Paracoccus denitrificans incorporated into vesicles with phospholipid reacts during turnover much as the oxidase from mitochondria does. The spectrophotometric changes observed at various wavelengths are closely similar, and the rate is about one-half of that for beef heart oxidase under the same conditions. The rate of appearance of oxidized cytochrome...
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The two-subunit cytochrome c oxidase from Paracoccus denitrificans has been sequentially digested with chymotrypsin and Staphylococcus aureus V8 protease. The smaller subunit of the enzyme (apparent Mr 32,000) was split into numerous peptides that were removed by anion-exchange HPLC. The larger subunit was only digested to a limited extent (from an apparent Mr 45,000 to Mr 43,000), and the spec...
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A highly active nitric oxide reductase was purified from Paracoccus denitrificans ATCC 35512, formerly named Thiosphaera pantotropha, which was anaerobically cultivated in the presence of nitrate. The enzyme was composed of two subunits with molecular masses of 34 and 15 kDa and contained two hemes b and one heme c per molecule. Copper was not found in the enzyme. The spectral properties sugges...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1980
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.77.1.196