T. Ikeda et al., ENZYME-CATALYZED ELECTROCHEMICAL OXIDATION OF D-GLUCONATE AT ELECTRODES COATED WITH D-GLUCONATE DEHYDROGENASE, A MEMBRANE-BOUND FLAVOHEMOPROTEIN, Journal of electroanalytical chemistry [1992], 352(1-2), 1993, pp. 267-278
D-gluconate dehydrogenase was dip coated onto ordinary electrodes of c
arbon paste, glassy carbon, pyrolytic graphite, gold, silver, platinum
or mercury. Surface redox waves clearly attributable to the reaction
of the adsorbed enzyme were not observed. Nevertheless, all the electr
odes with the adsorbed enzyme produced anodic currents for the electro
catalytic oxidation Of D-gluconate. Neither electron transfer mediator
s nor promoters were necessary. The adsorbed enzyme was stable enough
at pH 5.0 and at 5-degrees-C to allow the quantitative study of electr
ocatalysis. The current-potential curve for the catalytic oxidation re
action has an unusual shape, starting at - 0. 14 V with a hump at abou
t 0.02-0.05 V vs. Ag/AgCl. A steady state current was obtained at fixe
d electrode potentials and the current increased with increasing conce
ntrations of the substrate to approach saturation. The results could b
e described by an equation of direct bioelectrocatalysis at an electro
de coated with an enzyme. A probable candidate for the redox site of t
he enzyme that donates electrons to the electrode was heme c.