Direct electrochemistry of horseradish peroxidase immobilized on electrografted 4-ethynylphenyl film via click chemistry

Qin Ran; Ru Peng; Cong Liang; Siqiu Ye; Yuezhong Xian; Wenjing Zhang; Litong Jin

doi:10.1016/j.aca.2011.04.035

Direct electrochemistry of horseradish peroxidase immobilized on electrografted 4-ethynylphenyl film via click chemistry

Qin Ran, Ru Peng, Cong Liang, Siqiu Ye, Yuezhong Xian^*, Wenjing Zhang, Litong Jin

^*Corresponding author for this work

School of Chemistry and Molecular Engineering

East China Normal University

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

In this paper, a simple two-step approach for redox protein immobilization was introduced. Firstly, alkynyl-terminated film was formed on electrode surface by electrochemical reduction of 4-ethylnylphenyl (4-EP) diazonium compound. Then, horseradish peroxidase (HRP) modified with azido group was covalently immobilized onto the electrografted film via click reaction. Reflection absorption infrared (RAIR) spectroscopy and electrochemical methods were used to characterize the modification process. The results indicate that HRP retains its native structure and shows fast direct electron transfer. Moreover, the immobilized HRP shows excellent electrocatalytic reduction activity toward H₂O₂ with a linear range of 5.0×10^-6 to 9.3×10^-4molL^-1.

Original language	English
Pages (from-to)	27-31
Number of pages	5
Journal	Analytica Chimica Acta
Volume	697
Issue number	1-2
DOIs	https://doi.org/10.1016/j.aca.2011.04.035
State	Published - 4 Jul 2011

Keywords

Biosensor
Click chemistry
Diazonium salts
Direct electron transfer
Horseradish peroxidase

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10.1016/j.aca.2011.04.035

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title = "Direct electrochemistry of horseradish peroxidase immobilized on electrografted 4-ethynylphenyl film via click chemistry",

abstract = "In this paper, a simple two-step approach for redox protein immobilization was introduced. Firstly, alkynyl-terminated film was formed on electrode surface by electrochemical reduction of 4-ethylnylphenyl (4-EP) diazonium compound. Then, horseradish peroxidase (HRP) modified with azido group was covalently immobilized onto the electrografted film via click reaction. Reflection absorption infrared (RAIR) spectroscopy and electrochemical methods were used to characterize the modification process. The results indicate that HRP retains its native structure and shows fast direct electron transfer. Moreover, the immobilized HRP shows excellent electrocatalytic reduction activity toward H2O2 with a linear range of 5.0×10-6 to 9.3×10-4molL-1.",

keywords = "Biosensor, Click chemistry, Diazonium salts, Direct electron transfer, Horseradish peroxidase",

author = "Qin Ran and Ru Peng and Cong Liang and Siqiu Ye and Yuezhong Xian and Wenjing Zhang and Litong Jin",

year = "2011",

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doi = "10.1016/j.aca.2011.04.035",

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T1 - Direct electrochemistry of horseradish peroxidase immobilized on electrografted 4-ethynylphenyl film via click chemistry

AU - Ran, Qin

AU - Peng, Ru

AU - Liang, Cong

AU - Ye, Siqiu

AU - Xian, Yuezhong

AU - Zhang, Wenjing

AU - Jin, Litong

PY - 2011/7/4

Y1 - 2011/7/4

N2 - In this paper, a simple two-step approach for redox protein immobilization was introduced. Firstly, alkynyl-terminated film was formed on electrode surface by electrochemical reduction of 4-ethylnylphenyl (4-EP) diazonium compound. Then, horseradish peroxidase (HRP) modified with azido group was covalently immobilized onto the electrografted film via click reaction. Reflection absorption infrared (RAIR) spectroscopy and electrochemical methods were used to characterize the modification process. The results indicate that HRP retains its native structure and shows fast direct electron transfer. Moreover, the immobilized HRP shows excellent electrocatalytic reduction activity toward H2O2 with a linear range of 5.0×10-6 to 9.3×10-4molL-1.

AB - In this paper, a simple two-step approach for redox protein immobilization was introduced. Firstly, alkynyl-terminated film was formed on electrode surface by electrochemical reduction of 4-ethylnylphenyl (4-EP) diazonium compound. Then, horseradish peroxidase (HRP) modified with azido group was covalently immobilized onto the electrografted film via click reaction. Reflection absorption infrared (RAIR) spectroscopy and electrochemical methods were used to characterize the modification process. The results indicate that HRP retains its native structure and shows fast direct electron transfer. Moreover, the immobilized HRP shows excellent electrocatalytic reduction activity toward H2O2 with a linear range of 5.0×10-6 to 9.3×10-4molL-1.

KW - Biosensor

KW - Click chemistry

KW - Diazonium salts

KW - Direct electron transfer

KW - Horseradish peroxidase

UR - https://www.scopus.com/pages/publications/79957950541

U2 - 10.1016/j.aca.2011.04.035

DO - 10.1016/j.aca.2011.04.035

M3 - 文章

C2 - 21641415

AN - SCOPUS:79957950541

SN - 0003-2670

VL - 697

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EP - 31

JO - Analytica Chimica Acta

JF - Analytica Chimica Acta

IS - 1-2

ER -

Direct electrochemistry of horseradish peroxidase immobilized on electrografted 4-ethynylphenyl film via click chemistry

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Keywords

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