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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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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.
H, CONRAD, L, SMITH
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Cytochrome oxidase, ligands and electrons
Journal of Inorganic Biochemistry, 2005We present hereby an overview of the reactions of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, with ligands (primarily oxygen) and electrons, pointing out where necessary unresolved facts or questionable interpretations.
BRUNORI, Maurizio +2 more
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The “oxygenated complex” of cytochrome c oxidase
Biochemical and Biophysical Research Communications, 1972Abstract The conformational effects associated with the oxygenation of reduced cytochrome c oxidase have been investigated by Soret circular dichroism measurements of solutions at pH 7.2 and at 2°. The series of curves with increasing oxygenation indicates the formation of at least one distinct intermediate with an isodichroic point at 439 nm ...
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Proton pumping by cytochrome c oxidase
Nature, 1999Proton pumping by cytochrome c oxidase1 was thought to be restricted to the oxidative part of its catalytic cycle2, but this has been questioned3. New results4 were interpreted as an indication that two protons are pumped during the oxidative phase, and two during a subsequent reductive phase, and that this latter pumping is energetically coupled to ...
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Structure and function of cytochrome-c oxidase
Biochimie, 1986Recent works on the structure and the function of cytochrome-c oxidase are reviewed. The subunit composition of the mitochondrial enzyme depends on the species and is comprised of between 5 and 13 subunits. It is reduced to 1 to 3 subunits in prokaryotes. The complete amino acid composition has been derived from protein sequencing.
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Cytochrome c oxidase: A synopsis
Archives of Biochemistry and Biophysics, 1978M, Erecińska, D F, Wilson
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Cytochrome c oxidase deficiency
Biochemical Society Transactions, 1985DiMauro S. +6 more
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Bovine Heart Cytochrome c Oxidase
2000Mitochondrial cytochrome c oxidase reduces molecular oxygen (O2, hereafter) to water, and this process is coupled to the pumping of protons through the mitochondrial inner membrane from matrix space to intermembrane space (Ferguson-Miller and Babcock, 1996).
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