Characterization of cyanide binding to cytochrome c oxidase immobilized in electrode-supported lipid bilayer membranes

被引：11
|
作者：
Su, LY
Kelly, JB
Hawkridge, FM
Rhoten, MC
Baskin, SI
机构：
[1] Virginia Commonwealth Univ, Dept Chem, Richmond, VA 23284 USA
[2] Longwood Univ, Dept Nat Sci, Farmville, VA 23909 USA
[3] USA, Med Res Inst Chem Def, Aberdeen Proving Ground, MD 21010 USA
来源：
JOURNAL OF ELECTROANALYTICAL CHEMISTRY | 2005年 / 581卷 / 02期
基金：
美国国家科学基金会;
关键词：
cytochrome c oxidase; biosensor; cyanide dioxygen;
D O I：
10.1016/j.jelechem.2005.04.023
中图分类号：
O65 [分析化学];
学科分类号：
070302 ; 081704 ;
摘要：
Bovine cytochrome c oxidase has been successfully immobilized in elect rode-supported lipid bilayer membranes to investigate the effect of cyanide binding on the oxidation of ferrocytochrome c and the electroreduction of dioxygen. Cyanide binding to oxidase was found to be reversible and exhibited 1: 1 stoichiometry. Binding constants (K) were also determined for binding of cyanide to the reduced (62 mu M) and oxidized (195 mu M) forms of the oxidase. The cytochrome c oxidase-modified electrodes described here could potentially be used as an amperometric biosensor for the detection of cyanide. (c) 2005 Elsevier B.V. All rights reserved.
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页码：241 / 248
页数：8
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