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Study of Brain Cells in Neurodegenerative Diseases: Raman Microspectroscopy and Scanning Ion-Conductance Microscopy. [PDF]
Sovrem Tekhnologii MedMorozova KI +8 more
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Sources of non-Arrhenius electron transport in bacterial nanowires.
Phys Chem Chem PhysTerai K, Zhang P, Beratan DN.
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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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International Journal of Biochemistry, 1978
Abstract Enzymatic methylation of 72 lysyl residue of cytochrome c in lower organisms facilitates its binding to mitochondria, and subsequently plays an important role in the electron transport ...
E, Polastro +4 more
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Abstract Enzymatic methylation of 72 lysyl residue of cytochrome c in lower organisms facilitates its binding to mitochondria, and subsequently plays an important role in the electron transport ...
E, Polastro +4 more
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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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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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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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