INFLUENCE OF SULFHYDRYL REAGENTS ON THE CYTOCHROME c-CYTOCHROME OXIDASE SYSTEM
نویسندگان
چکیده
منابع مشابه
Influence of sulfhydryl reagents on the cytochrome c-cytochrome oxidase system.
Earlier papers (1,2) from this laboratory demonstrated that basic phenylmercuric nitrate depressed the cytochrome c-cytochrome oxidase system, determined manometrically, as well as yeast respiration (3) and bacterial growth (4), and that protection against these depressions could be afforded by sulfhydryl compounds (24) which, however, would not reverse the depression once it was established. I...
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Cytochrome c oxidase (EC 1.9.3.1) is the terminal enzyme of the mitochondria respiratory chain catalysing electron transfer from cytochrome c to molecular oxygen [ 1,2]. The molecular mechanism of this process is still not understood. At present, little is known about such important structural features as the position of the prosthetic groups or the location and characteristics of the cytochrom...
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Purified beef heart cytochrome c oxidase is inactivated to the extent of 35 to 50% by the nonpolar mercurial reagents mercuric chloride and ethylmercuric chloride. The inactivation is complete within 5 min. In titrations of activity, the plateau level of inactivation is attained at added ethylmercuric chloride:heme a ratios of about 1:1. Up to 3 mercury atoms/heme a are bound to the oxidase, al...
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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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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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1950
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)56332-8