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Single-molecule Mapping Of Long-range Electron Transport For A Cytochrome B(562) Variant.

Eduardo Antonio Della Pia, Q. Chi, D. D. Jones, J. E. MacDonald, J. Ulstrup, M. Elliott
Published 2011 · Chemistry, Medicine

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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 Å 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.

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