Results 231 to 240 of about 271,428 (260)

Dynamics of Protein-Protein Docking: Cytochrome c and Cytochrome c Peroxidase Revisited

Journal of Biomolecular Structure and Dynamics, 1998
The 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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Cytochrome c peroxidase binds two molecules of cytochrome c: Evidence for a low-affinity, electron-transfer-active site on cytochrome c peroxidase

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 ...
E D, Stemp, B M, Hoffman
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pH titration study of cytochrome c peroxidase and apocytochrome c peroxidase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978
A 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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Investigation of Electron Tunneling Between Cytochrome c Peroxidase and Cytochrome c

Science, 1978
The 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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The cytochrome c peroxidase of Paracoccus denitrificans

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
The 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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Preparation of cytochrome c peroxidase from baker's yeast

Analytical Biochemistry, 1977
Abstract A simple and readily reproducible procedure is presented for the preparation and purification of cytochrome c peroxidase from baker's yeast. Following autolysis of the yeast and extraction, the enzyme is collected on DEAE-cellulose at moderately high ionic strength, cluted, concentrated, and subjected to gel filtration in 0.1 m sodium ...
C E, Nelson, E V, Sitzman, C H, Kang, E, Margoliash   +3 more
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Interactions of Cytochrome c Peroxidase with Lysine Peptides

Biochemical and Biophysical Research Communications, 2000
Structural 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,
S, Hirota, T, Tsukazaki, O, Yamauchi
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[135] Cytochrome c and cytochrome c peroxidase from Pseudomonas fluorescens

1955
Publisher Summary This chapter discusses the determination of cytochrome c and cytochrome c peroxidase from Pseudomonas fluorescens . The cytochrome c obtained from Pseudomonas fluorescens is identical in spectrum to animal cytochrome c, but it differs from animal cytochrome c in some of its biochemical and adsorptive properties.
Howard M. Lenhoff, Nathan O. Kaplan
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The nature of complex formation between cytochrome c and cytochrome c peroxidase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
Abstract 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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A cytochrome c peroxidase isolated from Thiobacillus novellus

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
Abstract A cytochrome c peroxidase (ferrocytochrome c :H 2 O 2 oxidoreductase, EC 1.11.1.5) was isolated and highly purified from Thiobacillus novellus , and its properties were studied. The enzyme has haem c as the prosthetic group, and shows a peak at 398 nm in the oxidized form and peaks at 415, 520 and 550 nm in the reduced form.
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