Results 201 to 210 of about 138,479 (226)
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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.
K, Kim, J E, Erman
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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 ...
C W, Conroy, J E, Erman
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Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association
Science, 1988Brownian 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.
S H, Northrup, J O, Boles, J C, Reynolds
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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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Peroxidase activity of mitochondrial cytochrome c oxidase
Biochemistry (Moscow), 2007Mitochondrial 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.
T V, Vygodina, A A, Konstantinov
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Cytochrome c peroxidase from Methylococcus capsulatus Bath
Archives of Microbiology, 1997A bacterial cytochrome c peroxidase was purified from the obligate methanotroph Methylococcus capsulatus Bath in either the fully oxidized or the half reduced form depending on the purification procedure. The cytochrome was a homo-dimer with a subunit mol mass of 35.8 kDa and an isoelectric point of 4.5.
J A, Zahn +4 more
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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
Journal of Biomolecular NMR, 2013Here 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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Cytochrome c′-type cytochrome-c peroxidase derived from Nitrosomonas europaea
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986Abstract From Nitrosomonas europaea , a cytochrome c ′-type haem protein has been purified which has cytochrome- c peroxidase (ferrocytochrome- c :hydrogen-peroxide oxidoreductase, EC 1.11.1.5) activity. The protein has haem c and shows the high-spin-type absorption spectra: it shows absorption peaks at 400, 500 and 640 nm in the oxidized form ...
Takeshi Yamazaki +2 more
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Dynamics of Protein-Protein Docking: Cytochrome c and Cytochrome c Peroxidase Revisited
Journal of Biomolecular Structure and Dynamics, 1998The dynamics of the docking step in the electron transfer reaction between yeast cytochrome c peroxidase and iso-1-cytochrome c has been studied using the Brownian dynamics method. In particular we have calculated the bimolecular rate constant at which a specific complex, the xray crystalline complex, can form in solution by translational and ...
G, Castro, C A, Boswell, S H, Northrup
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