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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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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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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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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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pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978A pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase was carried out at 25 degrees C and 0.1 M ionic strength. The net charge on cytochrome c peroxidase due to proton association and dissociation varies from +32 at pH 2 to --50.2 at pH 12, while that of apocytochrome c peroxidase varies between +24.5 at pH 3 to --48 at pH 12 ...
James E. Erman, Curtis W. Conroy
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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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Ascorbate peroxidase activity of cytochromec
Free Radical Research, 2010The peroxidase-type reactivity of cytochrome c is proposed to play a role in free radical production and/or apoptosis. This study describes cytochrome c catalysis of peroxide consumption by ascorbate. Under conditions where the sixth coordination position at the cytochrome c heme iron becomes more accessible for exogenous ligands (by carboxymethylation,
Bischin, Cristina +6 more
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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.
Volkov, A.N., Van Nuland, Nico
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The cytochrome c peroxidase of Paracoccus denitrificans
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991The size, visible absorption spectra, nature of haem and haem content suggest that the cytochrome c peroxidase of Paracoccus denitrificans is related to that of Pseudomonas aeruginosa. However, the Paracoccus enzyme shows a preference for cytochrome c donors with a positively charged 'front surface' and in this respect resembles the cytochrome c ...
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