Marie-Christin Viehauser, MSc
Current position: PhD student
GMC-oxidoreductases are a major enzyme class targeted in biosensor development, because their substrates are physiologically and industrially relevant. Despite their variety of substrates, GMC-oxidoreductases have a conserved structure build around an FAD-binding Rossmann-fold. Cellobiose dehydrogenase (CDH) is a fungal extracellular flavocytochrome belonging to this enzyme family and one of the few oxidoreductases capable of direct electron transfer (DET).
The aim of this study is to attach the cytochrome domain from Neurospora crassa CDH IIA to several selected GMC oxidoreductases to generate chimeric enzymes with a build-in redox mediator. This principle occurs naturally in CDH and will be used to reroute the flow of electrons from the catalytic center to an electrode. The enzymes dependence on co-substrates like oxygen, quinones or redox mediators is to be replaced by direct electron transfer. These modified GMC oxidoreductases with efficient DET are highly interesting for biosensors and bioelectrocatalytic processes.