Redox potential of FAD-dependent glucose dehydrogenase

The redox potential is important to rationally employ oxidoreductases as bioelectrocatalysts to minimize electroactive interferences and maximize current density or cell voltage. For many FAD-dependent enzymes redox potentials are published, but not for FAD-dependent glucose dehydrogenase (GDH) from the glucose-methanolcholine (GMC)-oxidoreductase family, which are widely used in glucose biosensors. GDH is contacted via redox mediators or redox polymers and features a reasonably high substrate specificity and oxygen insensitivity. Here we report the redox potential of Glomerella cingulata GDH that was determined by two methods. Spectroelectrochemically we obtained a reduction potential of -0.265 +/- 0.003 V vs SHE and with the xanthine oxidase assay using Janus green B a potential of -0.267 +/- 0.016 V vs SHE. The determined redox potential of GcGDH differs greatly from that of Aspergillus niger glucose oxidase (-0.080 V vs SHE) despite an almost similar protein fold as GcGDH. Taking this excitingly low redox potential of GcGDH to develop optimized redox mediators and redox polymers for the fabrication of glucose oxidizing bioanodes with a low operating potential can drastically reduce the susceptibility of glucose biosensors towards electroactive substances or increase the cell voltage in biofuel cells.

Automated summary

The redox potential is important for the rational use of oxidoreductases as bioelectrocatalysts. In this study, the redox potential of glucose dehydrogenase (GDH), which is widely used in glucose biosensors, was determined. The low redox potential of GDH can be used to develop glucose oxidizing bioanodes with a low operating potential, reducing susceptibility to electroactive substances in glucose biosensors or increasing the cell voltage in biofuel cells.