Recent experimental data point to an asymmetric ground-state electronic distribution in the special pair (P) of purple bacterial reaction centers, which acts as the primary electron donor in photosynthesis. We have performed a density functional theory investigation on an extended model including the bacteriochlorophyll dimer and a few relevant surrounding residues to explore the origin of this asymmetry. We find strong evidence that the ground-state electron density in P is intrinsically asymmetric due to protein-induced distortions of the porphyrin rings, with excess electron charge on the P_Mbacteriochlorophyll cofactor. Moreover, the electron charge asymmetry is strongly modulated by the specific orientation of the C3¹ acetyl group, which is hydrogen bonded to His168. The electronic excitation has a significant charge transfer character inducing a displacement of electron charge from P_L to P_M, in agreement with experimental data in the excited state. These results are relevant for the understanding of the unidirectional electron transfer path in photosynthesis.