Results 191 to 200 of about 392,600 (216)
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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 ...
Kirana I. Dancheva +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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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.
R.A. Perreault +2 more
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Reactions of mercaptans with cytochrome c oxidase and cytochrome c
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 19801. The steady-state oxidation of ferrocytochrome c by dioxygen catalyzed by cytochrome c oxidase, is inhibited non-competitively towards cytochrome c by methanethiol, ethanethiol, 1-propanethiol and 1-butanethiol with Ki values of 4.5, 91, 200 and 330 microM, respectively. 2.
Ron Wever, J. Wilms, Johan Lub
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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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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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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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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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[7] Resolution of cytochrome-c oxidase
1986Publisher Summary This chapter focuses on the resolution of cytochrome- c oxidase. Cytochrome- c oxidase from bovine heart mitochondria is a multisubunit complex consisting of 13 polypeptides and four prosthetic groups, two hemes and two coppers. Heme is present only in the complexes that contain the major three subunits of cytochrome- c oxidase ...
Michael J. Corbley +3 more
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