Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

被引：119

作者：

Kharitonov, AB ^{[1
]}

Alfonta, L ^{[1
]}

Katz, E ^{[1
]}

Willner, I ^{[1
]}

机构：

[1] Hebrew Univ Jerusalem, Inst Chem, IL-91904 Jerusalem, Israel

来源：

JOURNAL OF ELECTROANALYTICAL CHEMISTRY | 2000年 / 487卷 / 02期

关键词：

NAD(+)-dependent enzymes; cytochrome c; cytochrome oxidase; impedance spectroscopy; chronopotentiometry; bioaffinity complex;

D O I：

10.1016/S0022-0728(00)00178-9

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interactions on surfaces between enzymes and their molecular or macromolecular cofactors. Alcohol dehydrogenase (E.C. 1.1.1.1.) and lactate dehydrogenase (E.C. 1.1.1.27) bind to an NAD(+)-functionalized monolayer electrode with association constants corresponding to 1.6 x 10(4) and 1.5 x 10(5) M-1, respectively. Cytochrome oxidase binds to an oriented cytochrome c monolayer assembled on an An electrode with an association constant of K-a= 1.2 x 10(7) M-1. (C) 2000 Elsevier Science S.A. All rights reserved.

引用

页码：133 / 141

页数：9

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