Electrochemical atomic force microscopy reveals potential stimulated height changes of redox responsive Cu-azurin on gold

Hairong Wu, Xueling Feng, B.D. Kieviet, Kaihuan Zhang, Henricus J.W. Zandvliet, G.W. Canters, Peter Manfred Schön, Gyula J. Vancso

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

Abstract

The redox active metalloprotein Cu-azurin was directly chemisorbed on bare gold electrodes through disulfide forming groups (Cys3Cys26). Topological and electrochemical properties of the immobilized molecules were investigated by electrochemical atomic force microscopy (EC-AFM) in Peak Force Tapping mode and cyclic voltammetry (CV). Cu-azurin layers showed surface confined reversible electrochemical behavior. In-situ EC-AFM studies revealed a height difference of 0.32 nm between the oxidized (+0.45 V) and the reduced state (−0.10 V) for Cu-azurin by imaging single molecules independent of the ionic strength of the buffer solution. In contrast, no height change was detected for Zn-azurin which is non-redox active and served as control. The observed height changes of the Cu-azurin upon electrochemical redox switching are thought to originate from conformational changes of the protein and the variation in the orientation of immobilized proteins between the oxidized and reduced states. In this manner, the height of the Cu-azurin could be modulated reversibly by the applied potential.
Original languageUndefined
Pages (from-to)529-537
JournalEuropean polymer journal
Volume83
DOIs
Publication statusPublished - 8 Dec 2016

Keywords

  • METIS-314570
  • IR-100116

Cite this

@article{080118c1e5254d3dab50811f3f07c1a3,
title = "Electrochemical atomic force microscopy reveals potential stimulated height changes of redox responsive Cu-azurin on gold",
abstract = "The redox active metalloprotein Cu-azurin was directly chemisorbed on bare gold electrodes through disulfide forming groups (Cys3Cys26). Topological and electrochemical properties of the immobilized molecules were investigated by electrochemical atomic force microscopy (EC-AFM) in Peak Force Tapping mode and cyclic voltammetry (CV). Cu-azurin layers showed surface confined reversible electrochemical behavior. In-situ EC-AFM studies revealed a height difference of 0.32 nm between the oxidized (+0.45 V) and the reduced state (−0.10 V) for Cu-azurin by imaging single molecules independent of the ionic strength of the buffer solution. In contrast, no height change was detected for Zn-azurin which is non-redox active and served as control. The observed height changes of the Cu-azurin upon electrochemical redox switching are thought to originate from conformational changes of the protein and the variation in the orientation of immobilized proteins between the oxidized and reduced states. In this manner, the height of the Cu-azurin could be modulated reversibly by the applied potential.",
keywords = "METIS-314570, IR-100116",
author = "Hairong Wu and Xueling Feng and B.D. Kieviet and Kaihuan Zhang and Zandvliet, {Henricus J.W.} and G.W. Canters and Sch{\"o}n, {Peter Manfred} and Vancso, {Gyula J.}",
year = "2016",
month = "12",
day = "8",
doi = "10.1016/j.eurpolymj.2015.12.002",
language = "Undefined",
volume = "83",
pages = "529--537",
journal = "European polymer journal",
issn = "0014-3057",
publisher = "Elsevier",

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Electrochemical atomic force microscopy reveals potential stimulated height changes of redox responsive Cu-azurin on gold. / Wu, Hairong; Feng, Xueling; Kieviet, B.D.; Zhang, Kaihuan; Zandvliet, Henricus J.W.; Canters, G.W.; Schön, Peter Manfred; Vancso, Gyula J.

In: European polymer journal, Vol. 83, 08.12.2016, p. 529-537.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Electrochemical atomic force microscopy reveals potential stimulated height changes of redox responsive Cu-azurin on gold

AU - Wu, Hairong

AU - Feng, Xueling

AU - Kieviet, B.D.

AU - Zhang, Kaihuan

AU - Zandvliet, Henricus J.W.

AU - Canters, G.W.

AU - Schön, Peter Manfred

AU - Vancso, Gyula J.

PY - 2016/12/8

Y1 - 2016/12/8

N2 - The redox active metalloprotein Cu-azurin was directly chemisorbed on bare gold electrodes through disulfide forming groups (Cys3Cys26). Topological and electrochemical properties of the immobilized molecules were investigated by electrochemical atomic force microscopy (EC-AFM) in Peak Force Tapping mode and cyclic voltammetry (CV). Cu-azurin layers showed surface confined reversible electrochemical behavior. In-situ EC-AFM studies revealed a height difference of 0.32 nm between the oxidized (+0.45 V) and the reduced state (−0.10 V) for Cu-azurin by imaging single molecules independent of the ionic strength of the buffer solution. In contrast, no height change was detected for Zn-azurin which is non-redox active and served as control. The observed height changes of the Cu-azurin upon electrochemical redox switching are thought to originate from conformational changes of the protein and the variation in the orientation of immobilized proteins between the oxidized and reduced states. In this manner, the height of the Cu-azurin could be modulated reversibly by the applied potential.

AB - The redox active metalloprotein Cu-azurin was directly chemisorbed on bare gold electrodes through disulfide forming groups (Cys3Cys26). Topological and electrochemical properties of the immobilized molecules were investigated by electrochemical atomic force microscopy (EC-AFM) in Peak Force Tapping mode and cyclic voltammetry (CV). Cu-azurin layers showed surface confined reversible electrochemical behavior. In-situ EC-AFM studies revealed a height difference of 0.32 nm between the oxidized (+0.45 V) and the reduced state (−0.10 V) for Cu-azurin by imaging single molecules independent of the ionic strength of the buffer solution. In contrast, no height change was detected for Zn-azurin which is non-redox active and served as control. The observed height changes of the Cu-azurin upon electrochemical redox switching are thought to originate from conformational changes of the protein and the variation in the orientation of immobilized proteins between the oxidized and reduced states. In this manner, the height of the Cu-azurin could be modulated reversibly by the applied potential.

KW - METIS-314570

KW - IR-100116

U2 - 10.1016/j.eurpolymj.2015.12.002

DO - 10.1016/j.eurpolymj.2015.12.002

M3 - Article

VL - 83

SP - 529

EP - 537

JO - European polymer journal

JF - European polymer journal

SN - 0014-3057

ER -