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The oxidation of cytochrome c by cytochrome c peroxidase

Archives of Biochemistry and Biophysics, 1960
Abstract 1. 1. The reaction between cytochrome c and cytochrome c peroxidase is first order in cytochrome c. 2. 2. The reaction is inhibited by both oxidized and reduced cytochrome c. 3. 3. The dependence of the reaction rate on ionic strength suggests that the reaction occurs at oppositely charged active sites on the two proteins. 4.
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A study of the kinetics of the oxidation of cytochrome c by cytochrome c oxidase

Archives of Biochemistry and Biophysics, 1956
Abstract 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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Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association

Science, 1988
Brownian dynamics computer simulations of the diffusional association of electron transport proteins cytochrome c (cyt c) and cytochrome c peroxidase (cyt c per) were performed. A highly detailed and realistic model of the protein structures and their electrostatic interactions was used that was based on an atomic-level spatial description.
S H, Northrup, J O, Boles, J C, Reynolds
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Cytochrome-c Oxidase

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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The Effect of Trifluoroacetyl-Cytochromecon the Cytochromec/CytochromecOxidase Reaction

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1981
The importance of electrostatic interactions to the reaction between cytochrome c and cytochrome c oxidase is indicated most directly by the rapid increase in Km as ionic strength is increased. However, Chessa et al. (1980, Hoppe-Seyler's Z. Physiol. Chem. 361, 1077--1091) have recently found that a cytochrome c derivative trifluoroacetylated at all 19
J, Gergerich, F, Millett
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Cytochrome c Peroxidase–Cytochrome c Complexes

2015
The yeast cytochrome c peroxidase (CCP)–cytochrome c (cytc) electron transfer system has been critically important in deciphering the molecular level details of protein–protein interactions and electron transfer. The crystal structure of the CCP–cytc together with a number mutagenesis, enzymological, and spectroscopic studies have provided a detailed ...
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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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Pulsed cytochrome c oxidase

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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Cytochromes c and Cytochrome c Containing Enzymes

1985
Porphyrin-containing compounds fulfil many different roles in biological systems. Broadly speaking, they fall into two main categories. There are the carrier molecules in which the substance carried is either oxygen, as in the case of the haemoglobins and myoglobins, or electrons, as in the cytochromes.
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