Highly Efficient Flavin-Adenine Dinucleotide Glucose Dehydrogenase Fused to a Minimal Cytochrome C Domain Academic Article uri icon


  • Flavin–adenine dinucleotide (FAD) dependent glucose dehydrogenase (GDH) is a thermostable, oxygen insensitive redox enzyme used in bioelectrochemical applications. The FAD cofactor of the enzyme is buried within the proteinaceous matrix of the enzyme, which makes it almost unreachable for a direct communication with an electrode. In this study, FAD dependent glucose dehydrogenase was fused to a natural minimal cytochrome domain in its c-terminus to achieve direct electron transfer. We introduce a fusion enzyme that can communicate with an electrode directly, without the use of a mediator molecule. The new fusion enzyme, with its direct electron transfer abilities displays superior activity to that of the native enzyme, with ak cat that is ca. 3 times higher than that of the native enzyme, ak cat/KM that is more than 3 times higher than that of GDH and 5 to 7 times higher catalytic …

publication date

  • December 6, 2017