منابع مشابه
The state of the copper in cytochrome c oxidase.
Nutritional studies have long supported the view that copper may be a part of cytochrome c oxidase (l-3). However, direct evidence did not become available until Eichel et al. (4) found that there was a good correlation between the copper content and the a-absorption by the reduced enzyme in fractions of heart mitochondria prepared with deoxycholate. More recently, Green et al. (5) and Okunuki ...
متن کاملCopper electron-nuclear double resonance of cytochrome c oxidase.
Electron-nuclear double resonance of copper was observed while monitoring the "intrinsic copper" electron paramagnetic resonance signal of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) near g = 2. This unambiguously establishes the presence of the metal (Cua) in the redox center responsible for this signal. The hyperfine couplings to copper are largely istropic and ...
متن کاملCopper chaperones for cytochrome c oxidase and human disease.
Biological processes in living cells are compartmentalized between lipid membranes. Integral membrane proteins often confer specific functions to these compartments and as such have a critical role in cellular metabolism and function. Cytochrome c oxidase is a macromolecular metalloprotein complex essential for the respiratory function of the cell. Elucidating the mechanisms of assembly of cyto...
متن کاملIntracytoplasmic Copper Homeostasis Controls Cytochrome c Oxidase Production
UNLABELLED Copper is an essential micronutrient used as a metal cofactor by a variety of enzymes, including cytochrome c oxidase (Cox). In all organisms from bacteria to humans, cellular availability and insertion of copper into target proteins are tightly controlled due to its toxicity. The major subunit of Cox contains a copper atom that is required for its catalytic activity. Previously, we ...
متن کاملCytochrome c oxidase.
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: 1959
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)69830-8