Factors Controlling the Substrate Specificity of Peroxidases: Kinetics and Thermodynamics of the Reaction of Horseradish Peroxidase Compound I with Phenols and Indole-3-acetic Acids
The rates of oxidation of reducing substrates by heme peroxidaseshave previously been thoughtto be controlled only by their ease of oxidation. In the presentstudy, we have compared the kinetics andthermodynamics of the oxidation of indole-3-acetic acid and derivativesand of phenols by horseradishperoxidase. Different dependencies of the reaction rates on thethermodynamic driving force reveal substratespecificity controlled by the enzyme-substrate complexes dissociationconstants (Michaelis-Mentenconstants) and by the reorganization energies of electron-transferwithin those complexes.