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
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.
UR - http://www.scopus.com/inward/record.url?scp=0034204643&partnerID=8YFLogxK
U2 - 10.1016/S0022-0728(00)00178-9
DO - 10.1016/S0022-0728(00)00178-9
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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 -