Electrochemical Behavior of Catechol Oxidation by H2O2 Using the Copper Binding Methanobactin as Mimetic Peroxidase

Abstract

The electrochemical behavior of catechol oxidation by H2O2which catalyzed by the copper binding methanobactin in aqueous solutions had been studied using cyclic voltammetry with a glassy carbon electrode. The contribution described the production and purification of a novel copper-binding peptide, methanobactin from Methylosinus trichosporium 3011, among which the copper binding methanobactin exhibited efficient horseradish peroxidase-like catalytic activity. The determinations of mimetic peroxidase activity in human/rat blood, garlic, onion and scallion serve as models for the proposed method. A comparison of the results with established classical analysis is satisfactory.