Naphthoquinone Derivatives As Low-Potential Electron Mediators of Fad-Dependent Glucose Dehydrogenase

Tuesday, October 13, 2015: 10:40
Borein B (Hyatt Regency)
D. P. Hickey, R. D. Milton, S. Abdellaoui, K. Lim, B. Tan (University of Utah), and S. D. Minteer (University of Utah)
Flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) is rapidly emerging as an alternative glucose-oxidizing enzyme in enzymatic fuel cells (EFCs).  FAD-GDH has the benefit over its commonly used counterpart, glucose oxidase (GOx), of not undergoing the parasitic reduction of O2 to H2O2, which can be troublesome in EFC applications. Additionally, the FAD cofactor has a relatively low redox potential in comparison to heme-based and PQQ-dependent enzymes, which can allow for a much higher theoretical cell potential. However, FAD-GDH is unable to facilitate rapid rates of direct electron transfer, and therefore requires a low-overpotential redox mediator to take full advantage of the low oxidation potential of its FAD cofactor.

We have prepared a range of naphthoquinone analogues that are capable of mediating electron transfer between FAD-GDH and carbon electrodes, with onset potentials ranging between -0.425 to -0.150 V (vs. SCE), at pH 7.4. Several naphthoquinone derivatives were immobilized either onto a poly(ethylenimine) backbone or directly onto the outer shell of FAD-GDH to yield a naphthoquinone redox hydrogel and a naphthoquinone-labeled FAD-GDH. Both methods demonstrated large catalytic current densities at low onset potentials. When coupled with an O2-reducing biocathode (bilirubin oxidase, direct electron transfer-type) the glucose/O2 EFC possessed a large open-circuit potential (OCP) of 0.864 V and was able to deliver a maximum current density of 5.4 mA cm-2. The EFC reached its maximum power density (2.3 mW cm-2) at 0.55 V.