Electrochemical behavior of catechol oxidation by H2O2 using the copper binding methanobactin as mimetic peroxidase
The electrochemical behavior ofcatechol 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.
Methanobactin Electrochemical Catalysis Mimetic peroxidase
Hua-nan Guan Jia-ying Xin Dan-dan Chen Chao-ze Yan Ying-xin Zhang Chun-gu Xia
Key Laboratory for Food Science and Engineering, Harbin University of Commerce, Harbin150076 Key Laboratory for Food Science and Engineering, Harbin University of Commerce, Harbin150076; State State Key Laboratory for Oxo Synthesis & Selective Oxidation, Lanzhou Institute of Chemical Physics,
国际会议
太原
英文
462-465
2012-06-23(万方平台首次上网日期,不代表论文的发表时间)