The interaction of three different c-type cytochromes with flavodoxin has been studied by computer graphics modelling and computational methods. Flavodoxin and each cytochrome can make similar hypothetical electron transfer complexes that are characterized by nearly coplanar arrangement of the prosthetic groups, close intermolecular contacts at the protein-protein interface, and complementary intermolecular salt linkages. Computation of the electrostatic free energy of each complex showed that all were electrostatically stable. However, both the magnitude and behavior of the electrostatic stabilization as a function of solution ionic strength differed for the three cytochrome c-flavodoxin complexes. Variation in the computed electrostatic stabilization appears to reflect differences in the surface distribution of all charged groups in the complex, rather than differences localized at the site of intermolecular contact. The computed electrostatic association constants for the complexes and the measured kinetic rates of electron transfer in solution show a remarkable similarity in their ionic strength dependence. This correlation suggests electrostatic interactions influence electron transfer rates between protein molecules at the intermolecular association step. Comparative calculations for the three cytochrome c-flavodoxin complexes show that these ionic strength effects also involve all charged groups in both redox partners.