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Photoreactions of Cytochrome c Oxidase
Photochemistry and Photobiology, 2006ABSTRACTThe photoreduction of oxidized bovine heart cytochrome c oxidase (CcO) by visible and UV radiation was investigated in the absence and presence of external reagents. In the former case, the quantum yields for direct photoreduction of heme A (heme a+ heme a3) were 2.6 ± 0.5 × 10−3, 4 ± 1 × 10−4, and 4 ± 2 × 10−6 with pulsed laser irradiation at ...
Ólöf Einarsdóttir, John S. Winterle
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A study of the kinetics of the oxidation of cytochrome c by cytochrome c oxidase
Archives of Biochemistry and Biophysics, 1956Abstract 1. 1. The kinetics of the oxidation of ferrocytochrome c by cytochrome c oxidase were studied spectrophotometrically by observing the rate of decrease in optical density at the α, β, or γ band of ferrocytochrome c as the reduced cytochrome c is oxidized. 2. 2.
Lucile Smith, Helen Conrad
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The kinetics of cytochrome c oxidase
Biochimica et Biophysica Acta, 1961Abstract 1. 1. The kinetics of the system: ascorbate-cytochrome c-cytochrome oxidase-oxygen, have been studied, using the Keilin and Hartree horse heart-muscle preparation. 2. 2. In disagreement with the general belief, the exogenous cytochrome c is not “nearly completely” reduced under the conditions of these measurements. 3. 3.
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Archives of Biochemistry and Biophysics, 1966
Abstract A study of the lipids contained in purified preparations of cytochrome c oxidase has been made. Other than the cholate which had been added as a solubilizing agent, only about 0.05 mg of lipid per milligram of protein was present. The phospholipid content did not exceed 9 μg per milligram protein in any preparation analyzed.
John Bright +2 more
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Abstract A study of the lipids contained in purified preparations of cytochrome c oxidase has been made. Other than the cholate which had been added as a solubilizing agent, only about 0.05 mg of lipid per milligram of protein was present. The phospholipid content did not exceed 9 μg per milligram protein in any preparation analyzed.
John Bright +2 more
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The Subunits of Cytochrome C Oxidase [PDF]
, 1982 Cytochrome c oxidase, the key to aerobic life, has been the subject of a number of excellent recent reviews written from general points of view (e.g., 1–14) and there is no need for another. However, within the last five years it has become apparent that the structures and functions of the subunits that comprise the enzyme hold the secrets to ultimate ...
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Cytochrome c oxidase deficiency [PDF]
Biochemical Society Transactions, 1985 DiMauro S. +6 more
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Reconstitution of Cytochrome c Oxidase
1986The reconstitution of coupled electron transport in cytochrome c oxidase is realized by removal of cholate from a starting suspension of purified complex (prepared as described by Errede et al. 1978) and a mixture of phospholipids. The reconstituted system so obtained (proteoliposomes) is constituted by small unilamellar vesicles with a diameter of 500–
S. Papa, N. Capitanio
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Cytochrome c oxidase: A synopsis
Archives of Biochemistry and Biophysics, 1978David F. Wilson, Maria Erecińska
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Cytochrome c Oxidase: Structure
1990The cytochrome oxidases are a wide and heterogeneous family of electron transfer hemoproteins which play a central role in the energy metabolism of aerobic organisms. They catalyze the terminal electron transfer steps in the complex branched respiratory systems of prokaryotes as well as in the mitochondrial respiratory chain [1].
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