Results 291 to 300 of about 203,240 (311)
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Ca2+ and the bacterial peroxidases: the cytochrome c peroxidase from Pseudomonas stutzeri
JBIC Journal of Biological Inorganic Chemistry, 2003The production of cytochrome c peroxidase (CCP) from Pseudomonas ( Ps.) stutzeri (ATCC 11607) was optimized by adjusting the composition of the growth medium and aeration of the culture. The protein was isolated and characterized biochemically and spectroscopically in the oxidized and mixed valence forms. The activity of Ps.
Francisco M. Gírio +8 more
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The nature of complex formation between cytochrome c and cytochrome c peroxidase
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1970Abstract 1. The nature of the forces involved in complex formation between cytochrome c and yeast cytochrome c peroxidase have been examined. 2. Polycations ( e.g. polylysine of 3000 and 150 000 mol. wt. and salmine) act as competitive inhibitors of cytochrome c peroxidation by cytochrome c peroxidase thereby supporting the previous ideas ...
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
The activation energy for the formation of the first red compound, ES, for cytochrome-c peroxidase (ferrocytochrome-c: hydrogen-peroxide oxidoreductase, EC 1.11.1.5) by i-propyl hydroperoxide and the rate constants for the formation of ES with various hydroperoxides have been determined.
S. Wold, T. Yonetani, P.-I. Ohlsson
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The activation energy for the formation of the first red compound, ES, for cytochrome-c peroxidase (ferrocytochrome-c: hydrogen-peroxide oxidoreductase, EC 1.11.1.5) by i-propyl hydroperoxide and the rate constants for the formation of ES with various hydroperoxides have been determined.
S. Wold, T. Yonetani, P.-I. Ohlsson
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Biochemical Journal, 2014
The peroxidase activity of cytochrome c may play a key role in the release of cytochrome c from the mitochondrial intermembrane space in the intrinsic apoptosis pathway.
T. Josephs +4 more
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The peroxidase activity of cytochrome c may play a key role in the release of cytochrome c from the mitochondrial intermembrane space in the intrinsic apoptosis pathway.
T. Josephs +4 more
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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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Electron transfer between cytochromec and cytochromec peroxidase
Journal of Bioenergetics and Biomembranes, 1995The reaction between cytochrome c (CC) and cytochrome c peroxidase (CcP) is a very attractive system for investigating the fundamental mechanism of biological electron transfer. The resting ferric state of CcP is oxidized by hydrogen peroxide to compound I (CMPI) containing an oxyferryl heme and an indolyl radical cation on Trp-191.
Bill Durham +3 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 ...
Charles A. Boswell +2 more
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Archives of Biochemistry and Biophysics, 1984
The interaction between cytochrome c and cytochrome c peroxidase was investigated using sedimentation equilibrium at pH 6,20 degrees C, in a number of buffer systems varying in ionic strength between 1 and 100 mM. Between 10 and 100 mM ionic strengths, the sedimentation of the individual proteins was essentially ideal, and sedimentation equilibrium ...
James E. Erman +2 more
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The interaction between cytochrome c and cytochrome c peroxidase was investigated using sedimentation equilibrium at pH 6,20 degrees C, in a number of buffer systems varying in ionic strength between 1 and 100 mM. Between 10 and 100 mM ionic strengths, the sedimentation of the individual proteins was essentially ideal, and sedimentation equilibrium ...
James E. Erman +2 more
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Photooxidation of Trp-191 in cytochrome c peroxidase by ruthenium-cytochrome c derivatives
Biochemistry, 1995A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC).
Mark A. Miller +4 more
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Interaction of cytochrome c peroxidase with cytochrome c
Biochemistry, 1974Takashi Yonetani, John J. Leonard
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