The electrochemical study of oxidation-reduction properties of horseradish peroxidase

被引：65

作者：

Li, JH ^{[1
]}

Dong, SJ ^{[1
]}

机构：

[1] CHINESE ACAD SCI, CHANGCHUN INST APPL CHEM, ELECTROANALYT CHEM LAB, CHANGCHUN 130022, PEOPLES R CHINA

来源：

JOURNAL OF ELECTROANALYTICAL CHEMISTRY | 1997年 / 431卷 / 01期

基金：

中国国家自然科学基金;

关键词：

horseradish peroxidase; self-assembled monolayers; direct electrochemistry of proteins;

D O I：

10.1016/S0022-0728(97)00158-7

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Oxidation-reduction properties of horseradish peroxidase (HRP) have been investigated by using direct electrochemical methods. Two successive separated distinct one-electron processes of HRP were obtained and the related physiological processes were described. The monolayer coverage of HRP at the electrode surface is about 50 pmol/cm(2). UV-Vis spectrophotometry and stable amperometry prove that the enzyme electrode possesses catalytic activity for H2O2 in the absence of a mediator and it might offer an opportunity to build the third generation of biosensors for analytes, such as H2O2, glucose and cholesterol etc. (C) 1997 Elsevier Science S.A.

引用

页码：19 / 22

页数：4

共 30 条

[1] ELECTRON-TRANSFER REACTION OF CYTOCHROME-C PEROXIDASE AT TIN OXIDE ELECTRODES [J].