Abstract
Protoporphyrin IX potentiates horseradish peroxidase-catalyzed hydrogen peroxide-mediated NADH oxidation, but the porphyrin cannot change the enzyme-catalyzed o-dianisidine oxidation. Spectrofluorimetric studies reveal that an interaction occurs between horseradish peroxidase and protoporphyrin IX. The interaction is predominantly hydrophobic and entropy-driven endothermic process. This interaction may influence the potentiation effect of the protoporphyrin IX on horseradish peroxidase-catalyzed NADH oxidation because the latter has a positive correlation with the extent of binding of the protein with the porphyrin.
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