Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

Andrei B. Kharitonov; Lital Alfonta; Eugenii Katz; Itamar Willner

doi:10.1016/S0022-0728(00)00178-9

Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

Andrei B. Kharitonov, Lital Alfonta, Eugenii Katz, Itamar Willner

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

117 Scopus citations

Abstract

Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interactions on surfaces between enzymes and their molecular or macromolecular cofactors. Alcohol dehydrogenase (E.C. 1.1.1.1.) and lactate dehydrogenase (E.C. 1.1.1.27) bind to an NAD⁺-functionalized monolayer electrode with association constants corresponding to 1.6×10⁴ and 1.5×10⁵ M^-1, respectively. Cytochrome oxidase binds to an oriented cytochrome c monolayer assembled on an Au electrode with an association constant of K_a = 1.2×10⁷ M^-1.

Original language	English
Pages (from-to)	133-141
Number of pages	9
Journal	Journal of Electroanalytical Chemistry
Volume	487
Issue number	2
DOIs	https://doi.org/10.1016/S0022-0728(00)00178-9
State	Published - 16 Jun 2000
Externally published	Yes

ASJC Scopus subject areas

Analytical Chemistry
General Chemical Engineering
Electrochemistry

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@article{64431c95df364733b363a35f7a855029,

title = "Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry",

abstract = "Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interactions on surfaces between enzymes and their molecular or macromolecular cofactors. Alcohol dehydrogenase (E.C. 1.1.1.1.) and lactate dehydrogenase (E.C. 1.1.1.27) bind to an NAD+-functionalized monolayer electrode with association constants corresponding to 1.6×104 and 1.5×105 M-1, respectively. Cytochrome oxidase binds to an oriented cytochrome c monolayer assembled on an Au electrode with an association constant of Ka = 1.2×107 M-1.",

author = "Kharitonov, {Andrei B.} and Lital Alfonta and Eugenii Katz and Itamar Willner",

note = "Funding Information: This research was supported by the Deutsche Forschungsgemeinschaft (DFG), Germany. The authors thank Dr A.B. Kotlyar for the gift of cytochrome oxidase and Dr Elena Panitkova for the assistance in the QCM measurements.",

year = "2000",

month = jun,

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doi = "10.1016/S0022-0728(00)00178-9",

language = "English",

volume = "487",

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journal = "Journal of Electroanalytical Chemistry",

issn = "0022-0728",

publisher = "Elsevier B.V.",

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TY - JOUR

T1 - Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

AU - Kharitonov, Andrei B.

AU - Alfonta, Lital

AU - Katz, Eugenii

AU - Willner, Itamar

N1 - Funding Information: This research was supported by the Deutsche Forschungsgemeinschaft (DFG), Germany. The authors thank Dr A.B. Kotlyar for the gift of cytochrome oxidase and Dr Elena Panitkova for the assistance in the QCM measurements.

PY - 2000/6/16

Y1 - 2000/6/16

N2 - Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interactions on surfaces between enzymes and their molecular or macromolecular cofactors. Alcohol dehydrogenase (E.C. 1.1.1.1.) and lactate dehydrogenase (E.C. 1.1.1.27) bind to an NAD+-functionalized monolayer electrode with association constants corresponding to 1.6×104 and 1.5×105 M-1, respectively. Cytochrome oxidase binds to an oriented cytochrome c monolayer assembled on an Au electrode with an association constant of Ka = 1.2×107 M-1.

AB - Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interactions on surfaces between enzymes and their molecular or macromolecular cofactors. Alcohol dehydrogenase (E.C. 1.1.1.1.) and lactate dehydrogenase (E.C. 1.1.1.27) bind to an NAD+-functionalized monolayer electrode with association constants corresponding to 1.6×104 and 1.5×105 M-1, respectively. Cytochrome oxidase binds to an oriented cytochrome c monolayer assembled on an Au electrode with an association constant of Ka = 1.2×107 M-1.

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U2 - 10.1016/S0022-0728(00)00178-9

DO - 10.1016/S0022-0728(00)00178-9

M3 - Article

AN - SCOPUS:0034204643

SN - 0022-0728

VL - 487

SP - 133

EP - 141

JO - Journal of Electroanalytical Chemistry

JF - Journal of Electroanalytical Chemistry

IS - 2

ER -

Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

Abstract

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