Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

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 t...

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Bibliographic Details
Published in:Journal of electroanalytical chemistry (Lausanne, Switzerland) Switzerland), 2000-06, Vol.487 (2), p.133-141
Main Authors: Kharitonov, Andrei B, Alfonta, Lital, Katz, Eugenii, Willner, Itamar
Format: Article
Language:English
Subjects:
Bioaffinity complex
Biological and medical sciences
Biosensors
Biotechnology
Chemistry
Chronopotentiometry
Cytochrome c
Cytochrome oxidase
Electrochemistry
Electrodes: preparations and properties
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
General and physical chemistry
Impedance spectroscopy
Ion selective electrodes
Methods. Procedures. Technologies
NAD +-dependent enzymes
Various methods and equipments
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Summary: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 1.6×10 4 and 1.5×10 5 M −1, respectively. Cytochrome oxidase binds to an oriented cytochrome c monolayer assembled on an Au electrode with an association constant of K a=1.2×10 7 M −1.
ISSN:1572-6657
1873-2569
DOI:10.1016/S0022-0728(00)00178-9