Most of my work aims at unravelling the properties of redox proteins immobilized on electrodes. In my early work I studied isolated proteins and enzymes such as cytochrome c, cytochrome P450, and [NiFe] hydrogenases by means of combined electrochemistry and surface-enhanced vibrational spectroscopic techniques (Raman and Infrared). In my current projects I apply this spectroelectrochemical approach to the study of redox proteins embedded in consortia of living cells such as microbial biofilms.
In parallel with these projects, I have been actively involved in the engineering of biocompatible electrode surfaces for spectroelectrochemical applications. Although most of these studies were often functional to the study of above mentioned redox proteins, I recently extended this approach to the study of ion channels incorporated on tethered bilayer lipid membranes .
Bioelectrochemistry is a well-established technique to study biological molecules ranging from isolated proteins and enzymes to microbial communities grown on electrodes. The main drawback of bioelectrochemistry as such is the lack of structural information. I overcome this limitation by performing electrochemical measurements in combination with various spectroscopic techniques on the same sample. This experimental strategy provides structural insights into the electrochemical properties of the system investigated.
Electron transfer in the bioelectrochemical systems I am currently studying are the molecular basis of electrical communication between electroactive microbial cells and metal electrodes. The analytical approach consists of electrochemistry (electro-microbiology) and surface-enhanced resonance Raman (SERR) spectroscopy. Progress in this field is expected to have a considerable impact in the field of sustainable energy production.