Single-Molecule Mapping of Long-range Electron Transport for a Cytochrome b562 Variant
Single-Molecule Mapping of Long-range Electron Transport for a Cytochrome b562 Variant
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DOI：
10.1021/nl103334q
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发表时间：
2011-01-01
期刊：
影响因子：
10.8
通讯作者：
Elliott, Martin
中科院分区：
文献类型：
--
作者：
Della Pia, Eduardo Antonio;Chi, Qijin;Elliott, Martin
细胞色素B（562）被改造为在表面暴露位置引入半胱氨酸残基，以促进在Au（111）表面上的直接自组装。受限的蛋白质表现出可逆的和快速的电子交换与金基板之间的距离为20埃的血红素氧化还原中心和金表面，一个明确的指示，建立了一个远程电子转移途径。电化学扫描隧道显微镜被用来映射在单分子水平上的蛋白质的电子传输功能。直接成像的Tunnel共振和测量表观分子电导，这两者都表现出强烈的氧化还原门控效应。这项研究解决了血红素蛋白的第一例，并在单分子生物电子学提供了新的视角。
Cytochrome b(562) was engineered to introduce a cysteine residue at a surface-exposed position to facilitate direct self-assembly on a Au(111) surface. The confined protein exhibited reversible and fast electron exchange with a gold substrate over a distance of 20 angstrom between the heme redox center and the gold surface, a clear indication that a long-range electron-transfer pathway is established. Electrochemical scanning tunneling microscopy was used to map electron transport features of the protein at the single molecule level. Tunneling resonance was directly imaged and apparent molecular conductance was measured, which both show strong redox-gated effects. This study has addressed the first case of heme proteins and offered new perspectives in single-molecule bioelectronics.