To elucidate how local molecular conformations play a role on electronic couplings for the long-range photoinduced charge-separated (CS) states in protein systems, we have analyzed time-resolved electron paramagnetic resonance (TREPR) spectra by polarized laser irradiations of 9,10-anthraquinone-1-sulfonate (AQ1S(-)) bound to human serum albumin (HSA). Analyses of the magnetophotoselection effects on the EPR spectra and a docking simulation clarified the molecular geometry and the electronic coupling of the long-range CS states of AQ1S(center dot 2-)-tryptophan214 radical cation (W214(center dot+)) separated by 1.2 nm. The ligand of AQ1S(-) has been demonstrated to be bound to the drug site I in HSA. Molecular conformations of the binding region were estimated by the docking Simulations, indicating that an arginine218 (R218(+)) residue bound to AQ1S(center dot 2-) mediates the long-range electron-transfer. The energetics of triad states of AQ1S(center dot 2-)-R218(+)-W214(center dot+) and AQ1S(-)-R218(center dot)-W214(center dot+) have been computed on the basis of the density functional molecular orbital calculations, providing the clear evidence for the long-range electronic couplings of the CS states in terms of the superexchange tunneling model through the arginine residue.