Results 161 to 170 of about 28,278 (208)
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Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association
Science, 1988Brownian 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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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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The Effect of Trifluoroacetyl-Cytochromecon the Cytochromec/CytochromecOxidase Reaction
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1981The 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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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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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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Cytochrome c Peroxidase–Cytochrome c Complexes
2015The 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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Cytochrome P450-like Substrate Oxidation Catalyzed by Cytochrome c and Immobilized Cytochrome c
Archives of Biochemistry and Biophysics, 1993Cytochrome c (cyt.c) was shown to catalyze cytochrome P450 (P450)-like oxidative reactions, such as N-, and O-demethylation, S-oxidation, and epoxidation of olefins. A more detailed examination showed that (i) N-methylcarbazole and thioanisole oxidation with H2(18)O2 catalyzed by cyt.c resulted in introduction of 18O into the product, and (ii) during ...
R, Akasaka, T, Mashino, M, Hirobe
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Cytochromes c and Cytochrome c Containing Enzymes
1985Porphyrin-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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Interaction of cytochrome c peroxidase with cytochrome c
Biochemistry, 1974J J, Leonard, T, Yonetani
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