Results 211 to 220 of about 74,519 (256)
Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association [PDF]
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.
Scott H. Northrup +2 more
openaire +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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
Francis Millett, Joseph Gergerich
openaire +3 more sources
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).
openaire +4 more sources
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).
openaire +4 more sources
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1969
Publisher Summary Yeast cytochrome c peroxidase, which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydroperoxide, was discovered in brewer's yeast by Altschul in 1940. Cytochrome c peroxidase is found exclusively in aerobically grown yeast.
openaire +5 more sources
Publisher Summary Yeast cytochrome c peroxidase, which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydroperoxide, was discovered in brewer's yeast by Altschul in 1940. Cytochrome c peroxidase is found exclusively in aerobically grown yeast.
openaire +5 more sources
A study of the kinetics of the oxidation of cytochrome c by cytochrome c oxidase
Archives of Biochemistry and Biophysics, 1956Abstract 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.
Lucile Smith, Helen Conrad
openaire +3 more sources
Biochimica et Biophysica Acta, 1960
Abstract In the present paper, the important role played by cytochrome c in the cytochrome oxidase system is demonstrated by using highly purified praparatinos of cytochromes a , c 1 , and c 1 . Despite the fact that cytochrome a can be rapidly reduced by p -phenylene-diamine, the component is not oxidized by oxyge if cytochrome c is not ...
Kazuo Okunuki +3 more
openaire +3 more sources
Abstract In the present paper, the important role played by cytochrome c in the cytochrome oxidase system is demonstrated by using highly purified praparatinos of cytochromes a , c 1 , and c 1 . Despite the fact that cytochrome a can be rapidly reduced by p -phenylene-diamine, the component is not oxidized by oxyge if cytochrome c is not ...
Kazuo Okunuki +3 more
openaire +3 more sources
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.
openaire +2 more sources
Cytochrome c interaction with membranes
Archives of Biochemistry and Biophysics, 1975Abstract A single species of tryptophan-59 formylated cytochrome c with a half-reduction potential of 0.085 ± 0.01 V at pH 7.0 was used to study its catalytic and functional properties. The spectral properties of the modified cytochrome show that the 6th ligand position is open to reaction with azide, cyanide, and carbon monoxide.
openaire +3 more sources
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1980
The oxidation of ferrocytochrome c mediated by cytochrome c oxidase was investigated in the presence of ferricytochrome c, trifluoroacetyl-cytochrome c, the heme fragments Hse65-[1-65] and Hse80-[1-80] and their respective porphyrin derivatives, as well as carboxymethylated apoprotein and related fragments, polycations, salts and neutral additives. The
Chessa G +5 more
openaire +4 more sources
The oxidation of ferrocytochrome c mediated by cytochrome c oxidase was investigated in the presence of ferricytochrome c, trifluoroacetyl-cytochrome c, the heme fragments Hse65-[1-65] and Hse80-[1-80] and their respective porphyrin derivatives, as well as carboxymethylated apoprotein and related fragments, polycations, salts and neutral additives. The
Chessa G +5 more
openaire +4 more sources
Structure of Cytochrome c Oxidase
Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1982[No abstract available]
R. A. Capaldi +2 more
openaire +4 more sources