[A network of hydrogen bonds in the reaction centers of Rhodobacter sphaeroides serves as a regulatory factor of the temperature dependence of the recombination rate constant of photooxidized bacteriochlorophyll and primary quinone acceptors].

The dark recombination rate constant for the photooxidized bacteriochlorophyll (P) and reduced primary quinone acceptor (QA) in the photosynthetic reaction centers (RC) from purple bacterium Rhodobacter sphaeroides depends nonmonotonically on temperature. The time of this reaction is approximately 100 ms at 270-300 K and decreases as the temperature both increases and decreases beyond this temperature range. It is known that the dome-shaped dependence of the thermodynamic stability on temperature is an intrinsic feature of many proteins in solution. The experimental results on the nonmonotonous temperature dependence of P+ and QA- recombination rate constant are discussed in terms of general thermodynamic approaches. The dynamic properties of the network of hydrogen bonds that are involved in the relaxation processes accompanying the electron transport are considered as a regulatory factor of the efficiency of electron transfer.