INVESTIGATION OF MECHANISMS OF PEROXIDASE-CATALYZED REACTIONS BY RADIATION-CHEMICAL TECHNIQUES

Haem peroxidases are globular proteins with an iron-porphyrin complex as prosthetic group. They catalyze the oxidation of substrate by perox ides, frequently via free-radical intermediates. The catalytic cycle i nvolves changes in the redox states of the prosthetic group that can b e monitored by changes in the intense absorption spectra. During the p ast decades, considerable scientific effort has been put into the eluc idation of the mechanisms of reactions catalyzed by these enzymes. Rad iation-chemical techniques have made an important contribution by prov iding information on the redox states of the enzymes and their interco nversions, as well as on the properties of the free-radical intermedia tes involved.