Electrostatic effects on the kinetics of oxidation-reduction reactions of c-type cytochromes

The kinetics of the oxidation-reduction reactions between horse heart cytochrome c, Euglena gracilis cytochrome c552, and ions (ascorbate, ferricyanide, and ferrocyanide) was investigated as a function of ionic strength at pH 7, 25 degrees C. The ionic strength was varied between 0.002 and 0.02 M. D...

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Bibliographic Details
Published in:The Journal of biological chemistry 1979-12, Vol.254 (24), p.12562-12566
Main Authors: Goldkorn, T, Schejter, A
Format: Article
Language:English
Subjects:
Animals
Ascorbic Acid
Cytochrome c Group - metabolism
Euglena
Ferricyanides
Ferrocyanides
Horses
Kinetics
Mathematics
Myocardium
Osmolar Concentration
Oxidation-Reduction
Protein Binding
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Summary:The kinetics of the oxidation-reduction reactions between horse heart cytochrome c, Euglena gracilis cytochrome c552, and ions (ascorbate, ferricyanide, and ferrocyanide) was investigated as a function of ionic strength at pH 7, 25 degrees C. The ionic strength was varied between 0.002 and 0.02 M. Data were analyzed according to four different functions of ionic strength. Results showed that the Kirkwood-Tanford smeared charge model holds well for the calculation of the activity coefficients and that the whole charges of these proteins are reflected in the rates of their reactions. Chemical modifications or changes in the pH that altered the charge of the proteins affected the primary salt effects as predicted by the smeared charge model.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(19)86351-2