“…Solvent reorganization effects, reduction-induced changes in the hydrogen bonding network within the hydration sphere of the cytochrome c and in protein flexibility are supposed to play the major role in determining the DS 0 rc values [4, 33, 36-38, 51, 52]. The negative DH 0 rc values, however, mostly arise from the stabilization of the ferroheme by ligand binding interactions and the hydrophobicity of the heme environment, but is also modulated by electrostatic interactions of the heme with protein surface and solution charges [4,33,[36][37][38][51][52][53]. The slight decrease in the E°0 values observed for the N ?…”