Two nonidentical forms of subunit V are functional in yeast cytochrome c oxidase.

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Two nonidentical forms of subunit V are functional in yeast cytochrome c oxidase.

In Saccharomyces cerevisiae, the inner mitochondrial membrane protein cytochrome c oxidase is composed of nine polypeptide subunits. Six of these subunits (IV, V, VI, VII, VIIa, VIII) are encoded by the nuclear genome, and the remaining three (I, II, III) are encoded by mitochondrial DNA. We report here the existence of two nonidentical subunit V polypeptides, which are encoded by separate gene...

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Cytochrome c Oxidase from Bakers’ Yeast

Cytochrome aa3 was purified 35to 40-fold from submitochondrial particles of commercial bakers’ yeast. The purification procedure involved solubilization of the enzyme with cholate, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose in the presence of Triton x-100. The purified, active enzyme contained approximately 10 nmoles of heme a per mg of protein and was free of oth...

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Cytochrome c Oxidase from Bakers’ Yeast

Purified cytochrome c oxidase from bakers’ yeast can be resolved into six polypeptide bands by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The apparent molecular weights of these components are I, 42,000; II, 34,500; III, 23,000; IV, 14,000; V, 12,500; and VI, 9,500. (Although Component V actually consists of two distinct polypeptide species, it will be regarde...

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Comparisons of subunit 5A and 5B isoenzymes of yeast cytochrome c oxidase

Subunit 5 of Saccharomyces cerevisiae cytochrome c oxidase (CcO) is essential for assembly and has two isoforms, 5A and 5B. 5A is expressed under normoxic conditions, whereas 5B is expressed at very low oxygen tensions. As a consequence, COX5A-deleted strains (Δcox5A) have no or only low levels of CcO under normoxic conditions rendering them respiratory deficient. Previous studies have reported...

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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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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1985

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.82.8.2235