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

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The electrochemical behavior of catechol oxidation by H2O2 which 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.

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462-465

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July 2012

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© 2012 Trans Tech Publications Ltd. All Rights Reserved

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