Results 251 to 260 of about 242,089 (307)
Disruption of testis-enriched cytochrome c oxidase subunit COX6B2 but not COX8C leads to subfertility. [PDF]
Exp AnimShimada K, Lu Y, Ikawa M.
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HyperTRCSS: A hyperspectral time-resolved compressive sensing spectrometer for depth-sensitive monitoring of cytochrome-c-oxidase and blood oxygenation. [PDF]
J Biomed OptLi NC, Ioussoufovitch S, Diop M.
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COA8 is a COX10-binding protein involved in the early biogenesis of cytochrome c oxidase
Brischigliaro M +13 more
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Current Opinion in Structural Biology, 1996
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-
C, Ostermeier, S, Iwata, H, Michel
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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-
C, Ostermeier, S, Iwata, H, Michel
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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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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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Structure of Cytochrome c Oxidase
Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1982[No abstract available]
R. A. Capaldi +2 more
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Cytochrome c oxidase deficiency
2002Publisher 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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Cytochrome c oxidase deficiency
American Journal of Medical Genetics, 2001AbstractCytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain, catalyzing the transfer of electrons from reduced cytochrome c to molecular oxygen. It is composed of 13 structural subunits, three of which are encoded in mtDNA and form the catalytic core of the enzyme.
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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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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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