Results 71 to 80 of about 27,803 (95)
Some of the next articles are maybe not open access.
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
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
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 ...
Paolo Sarti +9 more
openaire +3 more sources
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 ...
Paolo Sarti +9 more
openaire +3 more sources
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 ...
Reiko Akasaka +2 more
openaire +3 more sources
Biochemical and Biophysical Research Communications, 1980
Abstract [3H]-p-Azidophenacylbromide-(methyl-4-mercaptobutyrimidate)-cytochrome c from Saccharomyces cerevisiae was prepared and its properties determined. The radioactive photoaffinity-labeled cytochrome c was linked by irradiation into a covalent complex with cytochrome c oxidase.
David F. Wilson +2 more
openaire +3 more sources
Abstract [3H]-p-Azidophenacylbromide-(methyl-4-mercaptobutyrimidate)-cytochrome c from Saccharomyces cerevisiae was prepared and its properties determined. The radioactive photoaffinity-labeled cytochrome c was linked by irradiation into a covalent complex with cytochrome c oxidase.
David F. Wilson +2 more
openaire +3 more sources
[11] Hexadecaheme cytochrome c
1994Publisher Summary This chapter describes purification method and physicochemical data for hexadecaheme cytochrome c or high molecular weight cytochrome c (HMC) from Desulfovibrio vulgaris ( D. vulgaris ) Miyazaki (DvM) and D. vulgaris Hildenborough (DvH). For purification of hexadecaheme cytochrome c from DvH, wet cells are suspended in 2–2.
Yoshiki Higuchi +2 more
openaire +3 more sources