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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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Electrophoretically monodisperse cytochrome c oxidases
Biochemical and Biophysical Research Communications, 1988A discontinuous gradient polyacrylamide gel electrophoresis under nondenaturing conditions has been used to demonstrate monodispersity of procaryotic and eucaryotic cytochrome c oxidase preparations. Alkaline treated bovine enzyme which contains nine subunits as analysed by subsequent discontinuous SDS-polyacrylamide gel electrophoresis is a ...
M, Heinrichs, G, Buse
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Biogenesis of cytochrome c oxidase
Mitochondrion, 2005Cytochrome c oxidase (COX), the terminal enzyme of electron transport chains in some prokaryotes and in mitochondria, has been characterized in detail over many years. Recently, a number of new data on structural and functional aspects as well as on COX biogenesis emerged.
Oleh, Khalimonchuk, Gerhard, Rödel
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Charge interactions of cytochrome c with cytochrome c oxidase
International Journal of Biochemistry, 1984The pyridoxal phosphate (PLP) modification of the lysine amino groups in cytochrome c causes decrease in the reaction rate with cytochrome c oxidase. The rate constants for (PLP)2-cyt. c, PLP(Lys 86)-cyt. c, PLP(Lys 79)-cyt. c and native cytochrome c (at pH 7.4, I = 0.02) are 3.6 X 10(-3) sec-1, 5.5 X 10(-3) sec-1, 5.2 X 10(-3) sec-1 and 9.8 X 10(-3 ...
M I, Mitovska +2 more
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The cytochrome c binding site on cytochrome c oxidase
Biochemical and Biophysical Research Communications, 1979Abstract Cytochrome c was chemically coupled to cytochrome c oxidase using the reagent 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) which couples amine groups to carboxyl residues. The products of this reaction were analyzed on 2.5–27% polyacrylamide gradient gels electrophoretically.
C H, Seiter, R, Margalit, R A, Perreault
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Beef heart cytochrome c oxidase
Current Opinion in Structural Biology, 1997During the past two years, the crystal structures of beef heart cytochrome c oxidase with 13 subunits and the bacterial enzyme with four subunits have been reported at atomic resolution, ushering in a new era for cytochrome c oxidase research. Different proton pumping mechanisms have been proposed for the two organisms.
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Structure of Cytochrome c Oxidase
1980Cytochrome c oxidase or cytochrome c : oxygen oxidoreductase (CH 1.9.3.1) is the terminal oxidase in respiratory metabolism of all aerobic organisms and is responsible for catalyzing the reduction of dioxygen to water in the reaction: $$ 4{H^ + } + 4{e^ - } + {O_2} \rightleftarrows 2{H_2}O $$ The electrons for this reaction are provided by ...
R A, Capaldi, L, Prochaska, R, Bisson
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