The kinetics of electron transfer for rubredoxins are examined using density functional methods to determine the electronic structure characteristics that influence and allow for fast electron self-exchange in these electron-transport proteins. Potential energy surfaces for [FeX4](2-,1-) models confirm that the inner-sphere reorganization energy is inherently small for tetrathiolates (lambda(i)(ese) approximate to 0.1 eV), as evidenced by the only small changes in the equilibrium Fe-S bond distance during redox (Deltar(redox) approximate to 0.05 Angstrom). It is concluded that electronic relaxation and covalency in the reduced state allow for this small lambda(i)(ese) in this case relative to other redox couples, such as the tetrachloride. Using a large computational model to include the protein medium surrounding the [Fe(SCys)(4)](2-),(1-) active site in Desulfovibrio vulgaris Rubredoxin, the electronic coupling matrix element for electron self-exchange is defined for direct active-site contact (H-DA(0)). The simple Beratan-Onuchic model is used to extend coupling over the complete surface of the protein to provide an understanding of probable electron-transfer pathways. Regions of similar coupling properties are grouped together to define a surface coupling map, which reveals that very efficient self-exchange occurs only within 4 sigma-bonds of the active site. Longer-range electron transfer cannot support the fast rates of electron self-exchange observed experimentally. Pathways directly through the two surface cysteinate ligands dominate k(ese)(infinity) but surface-accessible amides hydrogen-bonded to the cysteinates also contribute significantly to the rate of electron self-exchange.