THE ELECTROCATALYTIC ENZYME FUNCTION OF ADSORBED CYTOCHROME-C PEROXIDASE ON PYROLYTIC-GRAPHITE

被引：43

作者：

SCOTT, DL ^{[1
]}

PADDOCK, RM ^{[1
]}

BOWDEN, EF ^{[1
]}

机构：

[1] N CAROLINA STATE UNIV,DEPT CHEM,RALEIGH,NC 27695

来源：

JOURNAL OF ELECTROANALYTICAL CHEMISTRY | 1992年 / 341卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0022-0728(92)80490-U

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Cytochrome c peroxidase (CCP) is a well characterized redox enzyme which can serve as a model for understanding the electrocatalytic function of adsorbed enzymes. Rotating disk electrode (RDE) voltammetry and cyclic voltammetry were used to show that CCP adsorbed on edge-oriented pyrolytic graphite reduces H2O2 electrocatalytically in a manner similar but not identical to solution CCP. Bulk electrolysis and Koutecky-Levich analysis of RDE data proved that the observed amperometric signal corresponds to the unmediated 2e- reduction of H2O2 to water. The pH dependence of the enzyme-substrate kinetics of adsorbed CCP were similar to those for solution CCP at pH less-than-or-equal-to 6 but showed some differences at pH > 6. RDE studies in solutions of varying ionic strength show that CCP remains strongly adsorbed to pyrolytic graphite even at high ionic strength. Preliminary cyclic voltammetry experiments revealed that adsorbed CCP is reversibly inhibited by inhibitors of solution CCP.

引用

页码：307 / 321

页数：15

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