Topological and electron-transfer properties of yeast cytochrome c adsorbed on bare gold electrodes

被引：45

作者：

Bonanni, B ^{[1
]}

Alliata, D ^{[1
]}

Bizzarri, AR ^{[1
]}

Cannistraro, S ^{[1
]}

机构：

[1] Univ Tuscia, Dipartimento Sci Ambientali, INFM, Biophys & Nanosci Grp, I-01100 Viterbo, Italy

来源：

CHEMPHYSCHEM | 2003年 / 4卷 / 11期

关键词：

chemisorption; metalloproteins; molecular dynamics; scanning probe microscopy; single-molecule studies;

D O I：

10.1002/cphc.200300784

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：

The redox metalloprotein yeast cytochrome c was directly self-chemisorbed on "bare" gold electrodes through the free sulfur-containing group Cys102. Topological, spectroscopic, and electron transfer properties of the immobilised molecules were investigated by in situ scanning probe microscopy and cyclic voltammetry. Atomic force and scanning tunnelling microscopy revealed individual protein molecules adsorbed on the gold substrate, with no evidence of aggregates. The adsorbed proteins appear to be firmly bound to gold and display dimensions in good agreement with crystallographic data. Cyclic voltammetric analysis showed: that up to 84% of the electrode surface is functionalised with electroactive proteins whose measured redox midpoint potential is in good agreement with the formal potential. Our results clearly indicate that this variant of cytochrome c is adsorbed on bare gold electrodes with preservation of morphological properties and redox functionality.

引用

页码：1183 / 1188

页数：6

共 43 条

[1] The transient nature of the diffusion controlled component of the electrochemistry of cytochrome c at 'bare' gold electrodes: an explanation based on a self-blocking mechanism [J].