The kinetics of the oxidation of iodide and ferrocyanide by compound I of horseradish peroxidase have been studied at 25 degrees C as a function of ionic strength and pH. The ionic strength dependencies of the second-order rate constants are tested with an extended form of the Debye-Hückel equation for the activity coefficients of the reacting species. For the reaction of iodide with compound I it is shown that the pH variation of the rate constant at zero ionic strength is caused mainly by titrating a catalytically important acid group and not mainly by the varying charge of the protein. The ferrocyanide reaction rate with compound I does not correlate with enzyme net charge, at all pH values. The influence of electrostatic interactions on reaction rates is discussed.
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Steiner et al. (1978) studied this question.
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