Contact glow discharge electrolysis (CGDE) can be exploited in environmental chemistry for the degradation of pollutants in wastewater. This study focuses on the employment of cheap materials (e.g., steel and tungsten) as electrodes for experiments of CGDE conducted in electrochemical cells with variable electrolytic composition. A clear correlation between breakdown voltage (VB)/discharge (or midpoint) voltage (VD) and the conductivity of the electrolyte is shown. Regardless of the chemical nature of the ionogenic species (acid, base or salt), the higher the conductivity of the solution, the lower the applied potential required for the onset of the glow discharge. Concerning practical application, these salts could be added to poorly conductive wastewaters to increase their conductivity and thus reduce the ignition potential necessary for the development of the CGDE. Such an effect could render the process of chemical waste disposal from wastewaters more economical. Moreover, it is evidenced that both VB and VD are practically independent on the ratio anode area to cathode area if highly conductive solutions are employed.

We apply an integrated approach combining microsecond MD simulations and (polarizable) QM/MM calculations of NMR, FTIR, and UV–vis spectra to validate the structure of the light-activated form of the AppA photoreceptor, an example of blue light using flavin (BLUF) protein domain. The latter photoactivate through a proton-coupled electron transfer (PCET) that results in a tautomerization of a conserved glutamine residue in the active site, but this mechanism has never been spectroscopically proven for AppA, which has been always considered as an exception. Our simulations instead confirm that the spectral features observed upon AppA photoactivation are indeed directly connected to the tautomer form of glutamine as predicted by the PCET mechanism. In addition, we observe small but significant changes in the AppA structure, which are transmitted from the flavin binding pocket to the surface of the protein.