In this paper we give an account of our ongoing effort to un -derstand bacterial photosynthesis at the atomic level. First, we de -scribe earlier simulations which investigate the nuclear motion cou -pled to the primary donor excitation in bacterial reaction centers (RC). Then, we discuss the molecular modeling of the chromophores of the RC of rhodobacter sphaeroides. Finally, we report on our latest molecular dynamics simulation results concerning a RC in a deter -gent micelle.The bacterial photosynthetic reaction center (RC)[1, 2] is a membrane protein composed of chromophores (bacteriochlorophylls, bacteriopheophytins and quinones) and three protein subunits named L, M and H. While pro teins L and M form two branches of the RC (almost the mirror images of each other) and provide the necessary scaffolding to hold in place bacteri ochlorophylls and bacteriopheophytins, the H subunit is in contact with the bacterial cytoplasm and binds the quinones in its interior. In the region of the RC near the pery-plasm is located a bacteriochlorophylls dimer, the socalled special pair (P). This chromophore is at the junction point between the L and M branches and is involved directly in the first photosynthetic electron transfer.Photosynthesis in purple bacteria commences with the excitation of P, the energy for such excitation being transferred directly from surrounding light harvesting proteins. The excited state P* then decays in a charge
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