Results 261 to 270 of about 242,089 (307)
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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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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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The kinetics of cytochrome c oxidase I. The system: Cytochrome c-cytochrome oxidase-oxygen
Biochimica et Biophysica Acta, 1961Abstract 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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Cytochrome c oxidase deficiency
Biochemical Society Transactions, 1985DiMauro S. +6 more
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