Oxidation of phenols by horseradish peroxidase and lactoperoxidase compound II--kinetic considerations.

Oxidation of para substituted phenols by horseradish peroxidase compound II (HRP-II) and lactoperoxidase compound II (LPO-II) were studied using stopped flow technique. Apparent second order rate constants (kapp) of the reactions were determined. The kinetics of oxidation of phenols by HRP-II and LPO-II have been compared with the oxidation potentials of the substrates. Reorganization energies of electron-transfer of phenols to the enzymes were estimated from the variation of second order rate constants with the thermodynamic driving force.

Spectrophotometric measurements on verdo-myoglobin: relevance to the oxidation of ferri-myoglobin by chlorite ion.

Spectrophotometric observations on verdo-myoglobin, reconstituted from apomyoglobin and verdo-heme and its oxidation products, are described. Relevance of these results to the oxidation of ferri-myoglobin by chlorite ion is also discussed.