Adsorption and Interfacial Electron Transfer of Saccharomyces Cerevisiae

Yeast Cytochrome c Monolayers on Au(111) Electrodes

Allan Glargaard Hansen, Anja Boisen, Jens Ulrik Nielsen, Hainer Wackerbarth, Ib Chorkendorff, Jens Enevold Thaulov Andersen, Jingdong Zhang, Jens Ulstrup

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

We have studied the adsorption and electron-transfer dynamics of Saccharomyces cerevisiae (yeast) iso-l-cytochrome c adsorbed on Au(lll) electrodes in aqueous phosphate buffer media. This cytochrome possesses a thiol group dos e to the protein surface (Cysl02) suitable for linking the protein to gold without drastic protein unfolding. A comprehensive approach, based on linear sweep and differential pulse voltammetry, capacitance measurements, X-ray photoelectron spectroscopy (XPS) , in situscanning tunneling microscopy (STM), and microcantilever sensor (MCS) techniques has been used. The voltammetric data display a thiol reductive desorption signal corresponding to dase to monolayer coverage. Reductive desorption is also reflected in a capacitance peak. Voltammetric signals from the heme group in both native and partially denatured states could also be detected. XPS shows dear Au -S band formation, but this observation is not condusive for aqueous buffer conditions, as the protein is extensively unfolded under ultrahigh vacuum conditions needed for XPS. In situ STM disdoses de ar sub-monolayer coverage to molecular resolution. Imaging is robust in a 0.2 V electrochemical potential range negative ofthe equilibrium potential of YCC, where the protein is electrochemically functional. The MCS data show tensile differential stress signals when YCC is adsorbed on a gold-coate d MCS, with distinguishable adsorption phases in the time range from <102 s to several thousand seconds. Comprehensive approaches to the mapping of adsorbed functional redox metalloproteins toward the single-molecule level, such as in the present study, will be important in the construction of nanoscale devices for multifarious biological and environmental screening.
Original languageEnglish
JournalLangmuir
Volume19
Issue number8
Pages (from-to)3419-3427
ISSN0743-7463
Publication statusPublished - 2003

Cite this

Hansen, Allan Glargaard ; Boisen, Anja ; Nielsen, Jens Ulrik ; Wackerbarth, Hainer ; Chorkendorff, Ib ; Andersen, Jens Enevold Thaulov ; Zhang, Jingdong ; Ulstrup, Jens. / Adsorption and Interfacial Electron Transfer of Saccharomyces Cerevisiae : Yeast Cytochrome c Monolayers on Au(111) Electrodes. In: Langmuir. 2003 ; Vol. 19, No. 8. pp. 3419-3427.
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title = "Adsorption and Interfacial Electron Transfer of Saccharomyces Cerevisiae: Yeast Cytochrome c Monolayers on Au(111) Electrodes",
abstract = "We have studied the adsorption and electron-transfer dynamics of Saccharomyces cerevisiae (yeast) iso-l-cytochrome c adsorbed on Au(lll) electrodes in aqueous phosphate buffer media. This cytochrome possesses a thiol group dos e to the protein surface (Cysl02) suitable for linking the protein to gold without drastic protein unfolding. A comprehensive approach, based on linear sweep and differential pulse voltammetry, capacitance measurements, X-ray photoelectron spectroscopy (XPS) , in situscanning tunneling microscopy (STM), and microcantilever sensor (MCS) techniques has been used. The voltammetric data display a thiol reductive desorption signal corresponding to dase to monolayer coverage. Reductive desorption is also reflected in a capacitance peak. Voltammetric signals from the heme group in both native and partially denatured states could also be detected. XPS shows dear Au -S band formation, but this observation is not condusive for aqueous buffer conditions, as the protein is extensively unfolded under ultrahigh vacuum conditions needed for XPS. In situ STM disdoses de ar sub-monolayer coverage to molecular resolution. Imaging is robust in a 0.2 V electrochemical potential range negative ofthe equilibrium potential of YCC, where the protein is electrochemically functional. The MCS data show tensile differential stress signals when YCC is adsorbed on a gold-coate d MCS, with distinguishable adsorption phases in the time range from <102 s to several thousand seconds. Comprehensive approaches to the mapping of adsorbed functional redox metalloproteins toward the single-molecule level, such as in the present study, will be important in the construction of nanoscale devices for multifarious biological and environmental screening.",
author = "Hansen, {Allan Glargaard} and Anja Boisen and Nielsen, {Jens Ulrik} and Hainer Wackerbarth and Ib Chorkendorff and Andersen, {Jens Enevold Thaulov} and Jingdong Zhang and Jens Ulstrup",
year = "2003",
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Adsorption and Interfacial Electron Transfer of Saccharomyces Cerevisiae : Yeast Cytochrome c Monolayers on Au(111) Electrodes. / Hansen, Allan Glargaard; Boisen, Anja; Nielsen, Jens Ulrik; Wackerbarth, Hainer; Chorkendorff, Ib; Andersen, Jens Enevold Thaulov; Zhang, Jingdong; Ulstrup, Jens.

In: Langmuir, Vol. 19, No. 8, 2003, p. 3419-3427.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Adsorption and Interfacial Electron Transfer of Saccharomyces Cerevisiae

T2 - Yeast Cytochrome c Monolayers on Au(111) Electrodes

AU - Hansen, Allan Glargaard

AU - Boisen, Anja

AU - Nielsen, Jens Ulrik

AU - Wackerbarth, Hainer

AU - Chorkendorff, Ib

AU - Andersen, Jens Enevold Thaulov

AU - Zhang, Jingdong

AU - Ulstrup, Jens

PY - 2003

Y1 - 2003

N2 - We have studied the adsorption and electron-transfer dynamics of Saccharomyces cerevisiae (yeast) iso-l-cytochrome c adsorbed on Au(lll) electrodes in aqueous phosphate buffer media. This cytochrome possesses a thiol group dos e to the protein surface (Cysl02) suitable for linking the protein to gold without drastic protein unfolding. A comprehensive approach, based on linear sweep and differential pulse voltammetry, capacitance measurements, X-ray photoelectron spectroscopy (XPS) , in situscanning tunneling microscopy (STM), and microcantilever sensor (MCS) techniques has been used. The voltammetric data display a thiol reductive desorption signal corresponding to dase to monolayer coverage. Reductive desorption is also reflected in a capacitance peak. Voltammetric signals from the heme group in both native and partially denatured states could also be detected. XPS shows dear Au -S band formation, but this observation is not condusive for aqueous buffer conditions, as the protein is extensively unfolded under ultrahigh vacuum conditions needed for XPS. In situ STM disdoses de ar sub-monolayer coverage to molecular resolution. Imaging is robust in a 0.2 V electrochemical potential range negative ofthe equilibrium potential of YCC, where the protein is electrochemically functional. The MCS data show tensile differential stress signals when YCC is adsorbed on a gold-coate d MCS, with distinguishable adsorption phases in the time range from <102 s to several thousand seconds. Comprehensive approaches to the mapping of adsorbed functional redox metalloproteins toward the single-molecule level, such as in the present study, will be important in the construction of nanoscale devices for multifarious biological and environmental screening.

AB - We have studied the adsorption and electron-transfer dynamics of Saccharomyces cerevisiae (yeast) iso-l-cytochrome c adsorbed on Au(lll) electrodes in aqueous phosphate buffer media. This cytochrome possesses a thiol group dos e to the protein surface (Cysl02) suitable for linking the protein to gold without drastic protein unfolding. A comprehensive approach, based on linear sweep and differential pulse voltammetry, capacitance measurements, X-ray photoelectron spectroscopy (XPS) , in situscanning tunneling microscopy (STM), and microcantilever sensor (MCS) techniques has been used. The voltammetric data display a thiol reductive desorption signal corresponding to dase to monolayer coverage. Reductive desorption is also reflected in a capacitance peak. Voltammetric signals from the heme group in both native and partially denatured states could also be detected. XPS shows dear Au -S band formation, but this observation is not condusive for aqueous buffer conditions, as the protein is extensively unfolded under ultrahigh vacuum conditions needed for XPS. In situ STM disdoses de ar sub-monolayer coverage to molecular resolution. Imaging is robust in a 0.2 V electrochemical potential range negative ofthe equilibrium potential of YCC, where the protein is electrochemically functional. The MCS data show tensile differential stress signals when YCC is adsorbed on a gold-coate d MCS, with distinguishable adsorption phases in the time range from <102 s to several thousand seconds. Comprehensive approaches to the mapping of adsorbed functional redox metalloproteins toward the single-molecule level, such as in the present study, will be important in the construction of nanoscale devices for multifarious biological and environmental screening.

M3 - Journal article

VL - 19

SP - 3419

EP - 3427

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 8

ER -