Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase

Hare, James F.; Ching, Edwin; Attardi, Giuseppe

doi:10.1021/bi00551a003

Cited by 98 publications

(33 citation statements)

References 47 publications

(65 reference statements)

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“…The present kinetic data show remarkable differences between the two enzymes. They suggest a regulatory role of the small, cytoplasmically synthesized polypeptides as previously postulated [21,24].…”

supporting

confidence: 63%

Kinetic and Structural Differences between Cytochrome c Oxidases from Beef Liver and Heart

Merle

Kadenbach

1982

European Journal of Biochemistry

106

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The cytochrome content of beef liver mitochondria differs from that of beef heart mitochondria by an eight‐ fold lower cytochrome aa3 and a twofold lower cytochrome b and c + c1 content. The kinetic properties of cytochrome c oxidases from beef liver and heart were measured with intact cytochrome c‐depleted membranes, deoxycholate‐dissolved membranes, and with the isolated enzymes at various cytochrome c concentrations with an oxygen electrode. Under all conditions a higher V was found for the liver enzyme, both for the low‐affinity and for the high‐affinity binding site for cytochrome c. Differences were also found for the Km of the two enzymes. Isolated beef heart mitochondria contained about twice as much cardiolipin than beef liver mitochondria. The isolated enzymes contained one mole cardiolipin per mole of the heart enzyme, but 2 moles cardiolipin per mole of the liver enzyme. By application of a high performance sodium dodecylsulfate gel electrophoretic system the two isolated enzymes could be separated into 13 different protein components, three of which (polypeptides VIa, VIIa and VIII) were found to differ in their apparent molecular weights. The functional meaning of cytochrome c oxidase iso‐ enzymes in liver and heart is discussed.

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supporting

confidence: 63%

Kinetic and Structural Differences between Cytochrome c Oxidases from Beef Liver and Heart

Merle

Kadenbach

1982

European Journal of Biochemistry

106

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“…Cytochrome c oxidase has been isolated from human tissue (placenta) and has been found to have essentially the same subunit composition as the beef heart enzyme (17). Therefore, it seemed likely that complex III from human and beef would be similar and, on this basis, antibodies were made against beef heart complex III for the purpose of identifying their counterparts in the human tissue.…”

Section: Resultsmentioning

confidence: 99%

Deficiency in ubiquinone cytochrome c reductase in a patient with mitochondrial myopathy and lactic acidosis.

Darley‐Usmar¹,

Kennaway²,

Buist³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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The skeletal muscle of a patient with a mitochondrial myopathy was examined. A defect in the electron transport chain was identified at the position of complex m by activity measurements and the low levels of reducible cytochrome b. The polypeptide composition of complex Ill in the patient's mitochondria was determined by antibody binding experiments. The method allowed detection of individual polypeptides at a lower limit of 10-40 ng of protein. Characterization of protein composition is thus possible by using a biopsy sample of 1 g of tissue. The level of core proteins, FeS protein, and subunit VI was greatly diminished in the patient's mitochondria. Cytochrome cl polypeptide was found at normal levels but was sensitive to proteolysis by trypsin. These results show that complex III is not assembled in the patient's mitochondria. The possible role of cytochrome b as the site of the primary lesion is discussed.

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“…The polypeptides are too small to be any of the known mitochondrially synthesized ATPase subunits, cytochrome c oxidase subunits, or cytochrome b (3,18,29). Their size is comparable to the dimer of the DCCD-binding protein, although a recent report suggests that this subunit is synthesized in the cytosol (19).…”

Section: Resultsmentioning

confidence: 99%

Assignment of two mitochondrially synthesized polypeptides to human mitochondrial DNA and their use in the study of intracellular mitochondrial interaction.

Oliver¹,

Wallace²

1982

Mol. Cell. Biol.

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Two mitochondrially synthesized marker polypeptides, MV-1 and MV-2, were found in human HeLa and HT1080 cells. These were assigned to the mitochondrial DNA in HeLa-HT1080 ybrids and hybrids by demonstrating their linkage to cytoplasmic genetic markers. These markers include mitochondrial DNA restriction site polymorphisms and resistance to chloramphenicol, an inhibitor of mitochondrial protein synthesis. In the absence of chloramphenicol, the expression of MV-1 and MV-2 in cybrids and hybrids was found to be directly proportional to the ratio of the parental mitochondrial DNAs. In the presence of chloramphenicol, the marker polypeptide linked to the chloramphenicol-sensitive mitochondrial DNA continued to be expressed. This demonstrated that resistant and sensitive mitochondrial DNAs can cooperate within a cell for gene expression and that the CAP-resistant allele was dominant or codominant to sensitive. Such cooperation suggests that mitochondrial DNAs can be exchanged between mitochondria.

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Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase

Cited by 98 publications

References 47 publications

Kinetic and Structural Differences between Cytochrome c Oxidases from Beef Liver and Heart

Kinetic and Structural Differences between Cytochrome c Oxidases from Beef Liver and Heart

Deficiency in ubiquinone cytochrome c reductase in a patient with mitochondrial myopathy and lactic acidosis.

Assignment of two mitochondrially synthesized polypeptides to human mitochondrial DNA and their use in the study of intracellular mitochondrial interaction.

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