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[Cytochrome C peroxidase].

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.
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Cytochrome C-mediated apoptosis.

Annual Review of Biochemistry, 2003
Apoptosis, or programmed cell death, is involved in development, elimination of damaged cells, and maintenance of cell homeostasis. Deregulation of apoptosis may cause diseases, such as cancers, immune diseases, and neurodegenerative disorders. Apoptosis
Xuejun Jiang, Xiaodong Wang
semanticscholar   +1 more source

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.
Lucile Smith, Helen Conrad
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Studies on cytochrome a

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
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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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Cytochrome c interaction with membranes

Archives of Biochemistry and Biophysics, 1975
Abstract 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.
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Sulfide inhibition of and metabolism by cytochrome c oxidase.

Biochemical Society Transactions, 2013
Hydrogen sulfide (H2S), a classic cytochrome c oxidase inhibitor, is also an in vitro oxidase substrate and an in vivo candidate hormonal ('gasotransmitter') species affecting sleep and hibernation.
P. Nicholls   +3 more
semanticscholar   +1 more source

Inhibition of the Cytochrome c/CytochromecOxidase System by CytochromecDerivatives and Related Fragments

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
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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 ...
Paolo Sarti   +9 more
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