Search

Bovine heart cytochrome c was studied through cyclic voltammetry in mixed water–organic solvent solutions under different conditions of temperature and the thermodynamic properties Δ S ° rc and Δ H ° rc calculated by the dependence of E ° by temperature. The effect of the organic fraction of the solvent on the E ° values of the native cyt c was found to be determined mainly by the decrease in dielectric constant of the medium. Specific interactions on the protein surface do not seem to play a remarkable role. The thermodynamic properties changes induced by the organic fraction have been interpreted tentatively in terms of solvation properties of cytochrome c and structural features of the protein environment.