Although cysteine is the preferred ligand for [Fe-S] core in case of iron-sulphur proteins, presence of other ligands together with cysteine is not uncommon. Being basically electron transfer proteins, redox potential of [Fe-S] core in these proteins in crucial to their functioning. Among other factors, charged nature of the microenvironment is believed to tune the redox potential. The iron-sulphur cluster, [Fe2S2(OC6H5)4]2−, has been investigated electrochemically in positive and negative microenvironments, both in solution and in film. Charge nature around the active centre has been found to affect its redox potential and diffusion coefficient significantly. In a film, where charges are more localized compared to solution, the effect on redox potential was more prominent.
