Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex. | Zendy

Takayuki Ozawa | Zendy; Hiroshi Suzuki | Zendy; Masashi Tanaka | Zendy

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Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex.

Author(s) -

Takayuki Ozawa,

Hiroshi Suzuki,

Masashi Tanaka

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.2.928

Subject(s) - cytochrome c oxidase , coenzyme q – cytochrome c reductase , cytochrome c1 , cardiolipin , chemistry , cytochrome c , cytochrome , electron transport complex iv , cytochrome c peroxidase , hemeprotein , oxidoreductase , heme , cytochrome b , biochemistry , chromatography , mitochondrion , membrane , enzyme , phospholipid , mitochondrial dna , gene

Cytochrome c oxidase (ferrocytochrome c oxygen oxidoreductase, EC 1.9.3.1) was purified from beef heart mitochondria by affinity chromatography. Phospholipids were removed by washing the oxidase with detergent on the affinity column; 1 mole of cardiolipin remained per mole of heme a. The oxidase was mixed with excess cytochrome c in 1.5% (wt/vol) cholate to form a complex. Slow removal of the detergent from the mixture by dialysis resulted in crystallization of cytochrome oxidase in the form of a 1:1 complex with cytochrome c. The chemical composition and spectrophotometric properties of the crystal are described. Increasing the solubility of a hydrophobic membrane protein by combination with hydropholic ligand is demonstrated as a maneuver for crystallizing the membrane protein.

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