Polymerization of o-Phenylenediamine Catalyzed byHemeproteins Encapsulated in Reversed Micelle

作     者：YANGYong MAOLu-yuan LILiu-zhu LIUXiao-guang SHIJun CAOShao-kui 

作者机构：LabofBiomimeticMacromoleculeCollegeofMaterialsEngineeringZhengzhouUniversityZhengzhou450052P.R.China 

出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)

年 卷 期：2004年第20卷第2期

页      面：240-243页

核心收录：

学科分类：1007[医学-药学(可授医学、理学学位)] 10[医学] 

基　　金：SupportedbytheNaturalScienceFundofHenanProvince(No.20024300006)andbytheNaturalScienceFundofHenanProvinceHighEducationofChina(No.0211021000) 

主　　题：Hemeprotein Hemoglobin Horseradish peroxidase Reversed micell o-Phenylenediamine 

摘      要：Hemeproteins encapsulated in reversed micelle formulated with di-2-ethylhexyl sulfosuccinate(AOT) was found to catalyze the polymerization of o-phenylenediamine(o-PDA) with hydrogen peroxide, whereas o-PDA catalyzed by hemeproteins dissolved in water could only form its trimers. As the nanostructural environment in reversed micelle acts as a certain orientation surrounding medium, it offers a strong electrostatic field that alters the reductive potential of Fe 3+/Fe 2+(E m7) in the heme of hemeproteins and thus increases the catalytic activity of peroxidase accordingly. According to the results of UV-Vis, 1H NMR and FTIR, the polymer catalyzed by hemoglobin(Hb) in reversed micelle was presumed to be constructed of lines and trapeziforms alternatively.