Electron Transfer and Electrocatalytic Properties of the Immobilized Met80Ala Cytochrome c Variant in Dimethylsulfoxide

• DOI: 10.1002/celc.202100499
• Publication Date: 2021-05-18T10:24:35Z
• Authors: Giulia Di Rocco; Beatrice Bighi; Marco Borsari; Carlo Augusto Bor...; Antonio Ranieri; Marco Sola; Gianantonio Batti...
• Keywords: Hemeprotein

Abstract The electrode‐immobilized Met80Ala variant of yeast iso‐1 cytochrome c in mixed water/dimethylsulfoxide (DMSO) solutions up to 60 % v/v DMSO shows thermodynamic and kinetic parameters electron exchange electrocatalytic properties towards O 2 reduction fully comparable those water. This is the result moderate protein conformational changes thanks immobilization that, a certain extent, preserves structure, possibly due constraints on mobility/flexibility induced by electrostatic interactions with electrode‐coating SAM. Upon increasing content solution beyond %, much larger perturbation occurs that leads progressive loss ability. Therefore, under these conditions, organic solvent remarkably affects structure probably involving major or even replacement 6 th axial hydroxide ligand heme iron strong ligand, lysine residue.