Results 261 to 270 of about 69,108 (276)
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Interactions of Cytochrome c Peroxidase with Lysine Peptides
Biochemical and Biophysical Research Communications, 2000Structural change of Cytochrome c peroxidase (CcP) due to interaction with lysine peptides (Lysptds) has been studied by absorption spectra and measurements on electron transfer between cytochrome c (cyt c) and CcP in the presence of Lysptd. Peaks were observed in the difference absorption spectrum of CcP between in the presence and absence of Lysptds,
Shun K. Hirota +3 more
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The catalytic mechanism of Pseudomonas cytochrome c peroxidase
Archives of Biochemistry and Biophysics, 1981Abstract The catalytic mechanism of Pseudomonas cytochrome c peroxidase has been studied using rapid-scan spectrometry and stopped-flow measurements. The reaction of the totally ferric form of the enzyme with H 2 O 2 was slow and the complex formed was inactive in the peroxidatic cycle, whereas partially reduced enzyme formed highly reactive ...
Marjaana Rönnberg +3 more
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Cytochrome c and cytochrome c peroxidase complex as studied by resonance Raman spectroscopy
Biochemistry, 1992Complex formation between ferricytochrome c peroxidase (CCP) and ferricytochrome c from yeast [cyt(Y)] and horse heart [cyt(H)] was studied by resonance Raman spectroscopy. On the basis of a detailed spectral analysis of the free proteins, it was possible to attribute changes in the spectra of the complexes to the individual proteins.
P. Hildebrandt +2 more
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Investigation of Electron Tunneling Between Cytochrome c Peroxidase and Cytochrome c
Science, 1978The nature of electron transfer between the bound complex cytochrome c and cytochrome c peroxidase has been investigated. Experimental verification of the predicted charge-transfer band provides evidence of electron tunneling as the mechanism of transfer between these molecules in solution at room temperature.
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Biochemistry, 1993
We have studied the affinity and stoichiometry of binding of cytochrome c (Cc) to zinc-substituted cytochrome c peroxidase [(ZnP)CcP], which is structurally and electrostatically equivalent to ferrous CcP. Transient absorption spectroscopy has been used to measure both the total quenching of the triplet-state (ZnP)CcP [3(ZnP)CcP] by Fe3+Cc and the ...
Brian M. Hoffman, Eric D. A. Stemp
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We have studied the affinity and stoichiometry of binding of cytochrome c (Cc) to zinc-substituted cytochrome c peroxidase [(ZnP)CcP], which is structurally and electrostatically equivalent to ferrous CcP. Transient absorption spectroscopy has been used to measure both the total quenching of the triplet-state (ZnP)CcP [3(ZnP)CcP] by Fe3+Cc and the ...
Brian M. Hoffman, Eric D. A. Stemp
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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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Biochemistry, 2000
Cytochrome c peroxidase (CcP) can bind as many as two cytochrome c (Cc) molecules in an electrostatic complex. The location of the two binding domains on CcP has been probed by photoinduced interprotein electron transfer (ET) between zinc-substituted horse cytochrome c (ZnCc) and CcP with surface charge-reversal mutations and by isothermal titration ...
Brian M. Hoffman +3 more
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Cytochrome c peroxidase (CcP) can bind as many as two cytochrome c (Cc) molecules in an electrostatic complex. The location of the two binding domains on CcP has been probed by photoinduced interprotein electron transfer (ET) between zinc-substituted horse cytochrome c (ZnCc) and CcP with surface charge-reversal mutations and by isothermal titration ...
Brian M. Hoffman +3 more
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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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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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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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