Results 251 to 260 of about 380,309 (295)
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Cytochrome a and Cytochrome Oxidase

Nature, 1938
A HEART muscle preparation obtained by a method previously described1 contains several dehydrogenases, a very powerful cytochrome oxidase and the three components (a, b, and c) of cytochrome. This material contains a high concentration of cytochrome a and is therefore very suitable for the study of this component.
D. KEILIN, E. F. HARTREE
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Structure of Cytochrome c Oxidase

Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1982
[No abstract available]
R. A. Capaldi   +2 more
openaire   +3 more sources

Pulsed cytochrome c oxidase

Journal of Inorganic Biochemistry, 1985
The identification of two functionally distinct states, called pulsed and resting, has led to a number of investigations on the conformational variants of the enzyme. However, the catalytic properties of cytochrome oxidase may depend on a number of experimental conditions related to the solvent as well as to the protocol followed to determine the ...
G. Antonini   +4 more
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Cytochrome-c Oxidase

2002
Cytochrome oxidase is the terminal oxidase of most of aerobic organisms and reduces molecular oxygen (O2) to water (1). The electrons and protons required for the formation of water molecules are transferred from both sides of the mitochondrial inner membranes in eukaryotic cells and of the cell membrane in prokaryotic cells (1).
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Association of cardiolipin and cytochrome oxidase

Biochemical and Biophysical Research Communications, 1970
Abstract A small amount of cardiolipin (diphosphatidyl glycerol) is tightly bound to cytochrome oxidase. The stoichiometry approaches one molecule of cardiolipin per molecule of cytochrome a. Solvent extraction and phospholipase treatments which remove or destroy other phospholipids and the bulk cardiolipin do not effect this tightly bound ...
Y C, Awasthi   +3 more
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Catalytic Mechanism of Cytochrome Oxidase

Nature, 1970
Kinetic experiments in a stopped-flow appartus provide evidence for multi-electron steps in the reduction of ...
E, Antonini   +3 more
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Cytochrome oxidase in health and disease

Gene, 2002
Yeast and bovine cytochrome c oxidases (COX) are composed of 12 and 13 different polypeptides, respectively. In both cases, the three subunits constituting the catalytic core are encoded by mitochondrial DNA. The other subunits are all products of nuclear genes that are translated on cytoplasmic ribosomes and imported through different transport routes
Antoni, Barrientos   +5 more
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The kinetics of cytochrome c oxidase I. The system: Cytochrome c-cytochrome oxidase-oxygen

Biochimica et Biophysica Acta, 1961
Abstract 1. 1. The kinetics of cytochrome c oxidase were studied in the Keilin and Hartree heart-muscle preparation by measuring the disappearance of reduced cytochrome c spectrophotometrically. The results of Smith and Conrad were confirmed. 2. 2.
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Studies on the resolution of cytochrome oxidase

Journal of Bioenergetics and Biomembranes, 1981
Cytochrome oxidase has been resolved in acetic acid and high salt/detergent media. In 0.5% acetic acid, the smaller subunits of the enzyme are selectively extracted with retention of an insoluble protein fraction containing subunits I-IV, VII. This fraction retains all the heme and copper of the original enzyme in a spectrally unaltered state, and ...
M, Fry, D E, Green
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Cytochrome c oxidase deficiency

2002
Publisher Summary Cytochrome c oxidase (COX) is the terminal component (complex IV) of the mitochondrial respiratory chain, the main energy-generating system of eukaryotic cells. COX-synthetic pathways have been derived from biochemical and genetic studies of respiratory-defective petite mutants of Saccharomyces cerevisiae .
Giacomo P, Comi   +3 more
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