Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry

Citation
Ab. Kharitonov et al., Probing of bioaffinity interactions at interfaces using impedance spectroscopy and chronopotentiometry, J ELEC CHEM, 487(2), 2000, pp. 133-141
Citations number
40
Categorie Soggetti
Spectroscopy /Instrumentation/Analytical Sciences
Journal title
JOURNAL OF ELECTROANALYTICAL CHEMISTRY
ISSN journal
15726657 → ACNP
Volume
487
Issue
2
Year of publication
2000
Pages
133 - 141
Database
ISI
SICI code
Abstract
Faradaic impedance spectroscopy and chronopotentiometry are used as electro chemical methods for probing in situ bioaffinity interactions on surfaces b etween enzymes and their molecular or macromolecular cofactors. Alcohol deh ydrogenase (E.C. 1.1.1.1.) and lactate dehydrogenase (E.C. 1.1.1.27) bind t o an NAD(+)-functionalized monolayer electrode with association constants c orresponding to 1.6 x 10(4) and 1.5 x 10(5) M-1, respectively. Cytochrome o xidase binds to an oriented cytochrome c monolayer assembled on an An elect rode with an association constant of K-a= 1.2 x 10(7) M-1. (C) 2000 Elsevie r Science S.A. All rights reserved.