Study on the Intermediate in the o-Phenylenediamine Oxidative Reaction Using Hemoglobin as A Mimetic Peroxidase in Aqueous-Organic Two Phase

作     者：Li Hai-cheng Li De-jia Huang Bo Jin De-long Zou Guo-lin Li Hai-cheng, Li De-jia, Huang Bo, Jin De-long, Zou Guo-lin  College of Life Sciences, Wuhan University, Wuhan 430072,Hubei, China

作者机构：College of Life Sciences Wuhan University Wuhan 430072 Hubei China 

出 版 物：《Wuhan University Journal of Natural Sciences》 (武汉大学学报（自然科学英文版）)

年 卷 期：2002年第7卷第1期

页      面：117-121页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 

基　　金：Supported by the National Natural Science F oundation of China( No.39770 2 0 0 ) 

主　　题：hemoglobin mimetic enzyme intermediate two phase reaction mechanism 

摘      要：Hemoglobin was used as a mimetic enzyme for peroxidase to catalyze the oxidative reaction of o-phenylenediamine with H2O2 which functioned as an oxidant. The relationship between physicochemical properties of the intermediate and enzymatic activity of hemoglobin was studied. Since the solubility of the intermediate in the reaction is higher in butanol phase than in water phase, the intermediate itself diffused from the aqueous phase to the butanol phase. The experimental results showed that the rate of product and the stability of intermediate were associated with the temperature and the pH value of the buffer. The formation rate of intermediate and half-life period reveal the maximal in pH7, nevertheless, the whole rate of the catalytic reaction is the greatest in pH5, which the ratio of the initial rate in final product formation compared to that intermediate formation is the greatest.