The reaction center (RC) of purple bacteria is formed by three protein subunits (L, M, and H) bound with four bacteriochlorophyll (Bchl) molecules, two bacteriopheophytin (Bph) molecules, two quinone ( Q A and Q B ) molecules, and one atom of nonheme iron. Two of the four Bchl molecules for a special pair P (Bchl dimer), which is a primary electron donor.After excitation of the P electron, it is transferred along the active A-chain, leading to consecutive formation of the anion radicals Bchl -, Bph -, and during 3, 0.9, and 200 ps, respectively [1][2][3]. In the excited state, P forms a dipole, the base of which ( d ) is approximately 0.6 Å; the base of the dipole (Bchl -Bchl + )*, the charge-transfer state of the dimer P, is 5-7 Å; and the base of the ion-radical pair P + Bchl -is approximately 17 Å. Dipoles or individual charges are sources of electric field; the latter interacts with charged atoms or atomic groups of water-protein environment and induces its rearrangement. It is known that the duration of rearrangement of hydrogen bonds is 10 -13 -10 -12 s [4,5]. It can be expected that the protons of the water-protein environment are primary messengers in the interaction between the electronegative (positive) state of cofactors and the medium within the femto-to picosecond time interval.In RCs isolated from the purple bacterium Rhodobacter sphaeroides , the excitation of the primary electron donor P is accompanied by bleaching of absorption bands at 870 and 600 nm. The exposure of the singlet excited state P + to an probing pulse resulted in a stimulated emission at 920 nm. Separation of charges P* Bchl → P + Bchl -is accompanied by a simultaneous decrease in the intensity of stimulated emission at 920 nm, bleaching of the absorption band of Bchl at Q A -800 nm, and appearance of a new absorption band at 1020 nm, ascribed to Bchl - [6,7]. Further transfer of the electron from Bchl -to Bph is monitored by the decrease in the absorption band at 760 nm, increase in the absorption band at 665 nm (Bph → Bph -), partial relaxation of absorption at 800 nm (Bchl -→ Bchl), and almost complete disappearance of absorption at 1020 nm (Bchl − → Bchl). It may be expected that the formation of states P*, P + , Bchl -, and Bph -will be reflected on the time course of spectral and amplitude characteristics of differential absorption spectra of these components of RC, including the femto-and picosecond time intervals, reflecting the interaction between unsteady states of cofactors and protons of water-protein environment. Figure 1 shows time-resolved differential absorption spectra of native preparations of Rb. sphaeroides RCs suspended in 10 mM sodium-phosphate buffer (pH 8.0), which were excited at room temperature at 600 nm with 70-fs light pulses at different temporal delays of the outgoing light pulse relative to the excitatory one. The time course of differential absorption spectra was analyzed for transitions P → P* → P + (830-890 nm) and Bph → Bph -(730-790 nm). As seen from Fig. 1, spectral position of the maximum of ...