The Formation of Compound I of Lactoperoxidase and Horseradish Peroxidase. A Comparison.

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Abstract
The rate constants for the formation of compound I of lactoperoxidase and 2 isoenzymes of horseradish peroxidase, and various hydroperoxides were determined. Multivariate data analysis by the partial least square models in latent variables was used for simultaneous comparison of rate constants and hydroperoxide substituent properties. Activation energies were determined for compound I formation with H2O2 and isopropyl hydroperoxide and the 3 peroxidases. The rate of formation of compound I from horseradish peroxidase C2 is dominated by pKa [-log10 Ka]. There is a less pronounced effect of pKa on horseradish peroxidase A2:2 and lactoperoxidase, where the contributions of lipophilicity and steric hindrance are stronger.