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Electron transfer dynamics of Rhodopseudomonas viridis reaction centers with a modified binding site for the accessory bacteriochlorophyll.

Femtosecond spectroscopy in combination with site-directed mutagenesis was used to study the influence of histidine L153 in primary electron transfer in the reaction center of Rhodopseudomonas viridis. Histidine was replaced by cysteine, glutamate, or leucine. The exchange to cysteine did not lead to significant changes in the primary reaction dynamics. In the case of the glutamate mutation, the decay of the excited electronic level of the special pair P* is slowed by a factor of 3. The exchange to leucine caused the incorporation of a bacteriopheophytin b instead of a bacteriochlorophyll b molecule at the BA site. As a consequence of this chromophore exchange, the energy level of the electron transfer state P+BA- is lowered to such an extent that repopulation from the next electron transfer intermediate state P+HA- takes place, resulting in a long-lasting P+BA- population. The observed differences in time constants are discussed in the scope of nonadiabatic electron transfer theory considering the influence of the amino acids at position L153 and the chromophore exchange on the energy level of the intermediate state P+BA-. The results show that the high efficiency of primary electron transfer is reduced substantially, if the energy level of P+BA- is lowered or raised by several hundred wave numbers.