Electron transfer kinetics of cytochrome c immobilized on a phenolic terminated thiol self assembled monolayer determined by scanning electrochemical microscopy

被引：12

作者：

Alizadeh, Vali ^{[1
]}

Mousavi, Mir Fazlollah ^{[1
]}

Mehrgardi, Masoud Ayatollahi ^{[2
]}

Kazemi, Sayed Habib ^{[3
]}

Sharghi, Hashem ^{[4
]}

机构：

[1] Tarbiat Modares Univ, Dept Chem, Tehran, Iran

[2] Univ Isfahan, Dept Chem, Esfahan, Iran

[3] Inst Adv Studies Basic Sci IASBS, Zanjan, Iran

[4] Shiraz Univ, Dept Chem, Shiraz, Iran

来源：

ELECTROCHIMICA ACTA | 2011年 / 56卷 / 17期

关键词：

Cytochrome c; Self assembled monolayer; Scanning electrochemical microscopy; 2-(2-Mercaptophenylnitrilomethylidyne)-phenol; IRON-SULFUR PROTEIN; HORSE HEART; ALKANETHIOL MONOLAYER; INORGANIC COMPLEXES; REDOX PROPERTIES; IONIC-STRENGTH; OXIDATION; REACTIVITIES; CONFORMATION; VOLTAMMETRY;

D O I：

10.1016/j.electacta.2011.03.029

中图分类号：

O646 [电化学、电解、磁化学];

学科分类号：

081704 ;

摘要：

In the present manuscript, the electrochemical behavior of cytochrome c (cyt-c) immobilized onto a phenolic terminated self assembled monolayer (SAM) on a gold electrode is investigated using cyclic voltammetry (CV) and scanning electrochemical microscopy (SECM). The tunneling electron transfer (ET) rate constant between the immobilized protein and the underlying electrode surface, and also the bimolecular ET rate constant between the immobilized protein and a probe has been obtained using approach curves that were obtained by SECM. The approach curves were recorded at different substrate overpotentials in the presence of various concentrations of ferrocyanide as a probe and various surface concentrations of cyt-c; then the standard tunneling ET and bimolecular rate constants are obtained as 3.4 +/- 0.3 s(-1) and (2.0 +/- 0.5) x 10(7) cm(3) mol(-1) s(-1), respectively. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：6224 / 6229

页数：6

共 37 条

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