Single-molecule Mapping of Long-range Electron Transfer for a Cytochrome b562 Variant

Eduardo Antonio Della Pia; Qijin Chi; D. Dafydd Jones; J. Emyr Macdonald; Jens Ulstrup; Martin Elliott

doi:10.1021/nl103334q

Single-molecule Mapping of Long-range Electron Transfer for a Cytochrome b562 Variant

Eduardo Antonio Della Pia, Qijin Chi, D. Dafydd Jones, J. Emyr Macdonald, Jens Ulstrup, Martin Elliott

Department of Chemistry

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

Cytochrome b562 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.

Original language	English
Journal	Nano Letters
Volume	11
Pages (from-to)	176-182
ISSN	1530-6984
DOIs	https://doi.org/10.1021/nl103334q
Publication status	Published - 2011

Keywords

Redox-gated tunneling resonance
Cytochrome b562
Protein engineering
Single-molecule electronics
Scanning tunneling microscopy
Nanobioelectronics

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10.1021/nl103334q

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@article{9050cf41edd64ae2b42dc09e6a2e51fc,

title = "Single-molecule Mapping of Long-range Electron Transfer for a Cytochrome b562 Variant",

abstract = "Cytochrome b562 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 {\AA} 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.",

keywords = "Redox-gated tunneling resonance, Cytochrome b562, Protein engineering, Single-molecule electronics, Scanning tunneling microscopy, Nanobioelectronics",

author = "{Della Pia}, {Eduardo Antonio} and Qijin Chi and Jones, {D. Dafydd} and Macdonald, {J. Emyr} and Jens Ulstrup and Martin Elliott",

year = "2011",

doi = "10.1021/nl103334q",

language = "English",

volume = "11",

pages = "176--182",

journal = "Nano Letters",

issn = "1530-6984",

publisher = "American Chemical Society",

}

TY - JOUR

T1 - Single-molecule Mapping of Long-range Electron Transfer for a Cytochrome b562 Variant

AU - Della Pia, Eduardo Antonio

AU - Chi, Qijin

AU - Jones, D. Dafydd

AU - Macdonald, J. Emyr

AU - Ulstrup, Jens

AU - Elliott, Martin

PY - 2011

Y1 - 2011

N2 - Cytochrome b562 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.

AB - Cytochrome b562 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.

KW - Redox-gated tunneling resonance

KW - Cytochrome b562

KW - Protein engineering

KW - Single-molecule electronics

KW - Scanning tunneling microscopy

KW - Nanobioelectronics

U2 - 10.1021/nl103334q

DO - 10.1021/nl103334q

M3 - Journal article

VL - 11

SP - 176

EP - 182

JO - Nano Letters

JF - Nano Letters

SN - 1530-6984

ER -