Results 211 to 220 of about 138,479 (226)

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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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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Cytochrome c Peroxidase−Cytochrome c Complex:  Locating the Second Binding Domain on Cytochrome c Peroxidase with Site-Directed Mutagenesis

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 ...
V W, Leesch, J, Bujons, A G, Mauk, B M, Hoffman   +3 more
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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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[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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Interaction of cytochrome c peroxidase with cytochrome c

Biochemistry, 1974
J J, Leonard, T, Yonetani
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Cytochrome-c peroxidase

1994
D. Schomburg, M. Salzmann, D. Stephan
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CROSS LINKING CYTOCHROME C TO YEAST CYTOCHROME C PEROXIDASE

Biochemical Society Transactions, 1981
G. W. Pettierew, S. Seilman
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Cytochrome-c peroxidase

2006
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