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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
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Journal of Physical Chemistry B, 2019
The immobilization of proteins on inorganic supports is attracting increasing interest since the realization of active surfaces finds application in enzyme-assisted catalysis, environmental sciences, and medical fields. In the present study, cytochrome c
L. Tarpani +5 more
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The immobilization of proteins on inorganic supports is attracting increasing interest since the realization of active surfaces finds application in enzyme-assisted catalysis, environmental sciences, and medical fields. In the present study, cytochrome c
L. Tarpani +5 more
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Biochemistry, 2019
Mitochondrial cytochrome c is a highly conserved protein in eukaryotes. Certain functions of cytochrome c have been tuned during evolution. For instance, the intrinsic peroxidase activity of human cytochrome c is much lower than that of the yeast ...
Haotian Lei +3 more
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Mitochondrial cytochrome c is a highly conserved protein in eukaryotes. Certain functions of cytochrome c have been tuned during evolution. For instance, the intrinsic peroxidase activity of human cytochrome c is much lower than that of the yeast ...
Haotian Lei +3 more
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Peroxidase activity of mitochondrial cytochrome c oxidase [PDF]
Biochemistry (Moscow), 2007 Mitochondrial cytochrome c oxidase is able to oxidize various aromatic compounds like o-dianisidine, benzidine and its derivatives (diaminobenzidine, etc.), p-phenylenediamine, as well as amidopyrine, melatonin, and some other pharmacologically and physiologically active substances via the peroxidase, but not the oxidase mechanism.
Alexander A. Konstantinov +1 more
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Journal of the American Chemical Society, 2017
In addition to serving as respiratory electron shuttle, ferri-cytochrome c (cyt c) acts as a peroxidase; i.e., it catalyzes the oxidation of organic substrates by H2O2. This peroxidase function plays a key role during apoptosis.
Victor C Yin, G. Shaw, L. Konermann
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In addition to serving as respiratory electron shuttle, ferri-cytochrome c (cyt c) acts as a peroxidase; i.e., it catalyzes the oxidation of organic substrates by H2O2. This peroxidase function plays a key role during apoptosis.
Victor C Yin, G. Shaw, L. Konermann
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The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c.
Dalton Transactions, 2018The peroxidase activity of cytochrome c is proposed to contribute to apoptosis by peroxidation of cardiolipin in the mitochondrial inner membrane. However, cytochrome c heme is hexa-coordinate with a methionine (Met80) on the distal side, stopping it ...
R. Parakra +3 more
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Methionine modification in cytochrome-c peroxidase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988Hydrogen peroxide oxidizes Met-119, Met-230 and Met-231 to the sulfoxide derivatives with equal initial rates in apocytochrome-c peroxidase at pH 4 in 0.1 M sodium acetate buffer. No detectable oxidation of Met-163 and Met-172 occurs under these conditions.
James E. Erman, Kyudon Kim
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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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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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Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction [PDF]
Journal of Biomolecular NMR, 2013 Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution.
A. Volkov, N. Nuland
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The oxidation of cytochrome c by cytochrome c peroxidase
Archives of Biochemistry and Biophysics, 1960Abstract 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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