Electrochemistry of Metalloproteins Attached through Functional Self-Assembled Monolayers on Gold and Ferromagnetic Electrodes

被引：8

作者：

Mondal, Prakash Chandra ^{[1
,3
]}

Fontanesi, Claudio ^{[1
,2
]}

机构：

[1] Weizmann Inst Sci, Dept Chem Phys, IL-76100 Rehovot, Israel

[2] Univ Modena & Reggio Emilia, DIEF, Via Vivarelli 10, I-41125 Modena, Italy

[3] Univ Alberta, Natl Inst Nanotechnol, Edmonton, AB T6G 2M9, Canada

来源：

CHEMPHYSCHEM | 2018年 / 19卷 / 01期

基金：

以色列科学基金会;

关键词：

charge transfer; cofactors; electronic coupling; metalloproteins; self-assembly; CYTOCHROME-C-OXIDASE; SPIN-DEPENDENT ELECTROCHEMISTRY; LIPID-BILAYER MEMBRANES; CHIRAL MOLECULES; SURFACE; PEPTIDES; NANOPARTICLES; HEMOGLOBIN; MECHANISM; TRANSPORT;

D O I：

10.1002/cphc.201701018

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We report the experimental results of a study of the electron-transfer processes of redox-active metalloproteins bound to mixed self-assembled monolayers (SAMs) on magnetic (nickel or ultrathin gold-coated nickel) or nonmagnetic (gold) electrodes. Metalloproteins, such as hemoglobin (Hb), CytochromeC (CytC), and CytC oxidase, are attached through electrostatic interactions to the free carboxylate or imidazole groups present in the mixed SAMs. The formation of both mixed SAMs and SAM/metalloprotein heterostructures were confirmed by using advanced surface analysis techniques, such as polarization modulation infrared reflection absorption spectroscopy and aqueous contact angle measurements. Electrochemical measurements indicated a stronger electronic coupling between Hb and CytC oxidase and the mixed-SAM-coated gold or gold-coated-nickel electrodes, whereas a weaker coupling was found between the protein and the pure nickel electrode. Surface coverage and the electron-transfer rate constant were estimated from the cyclic voltammetry data.

引用

页码：60 / 66

页数：7

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