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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 acceptorsстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Krasilnikov P.M., Bashtovyi D., Knox P.P., Pashchenko V.Z.
- Журнал: Biophysics
- Том: 49
- Номер: 5
- Год издания: 2004
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 751
- Последняя страница: 756
- Аннотация: The dark recombination rate constant for the photooxidized bacteriochlorophyll (P) and reduced primary quinone acceptor (Q(A)) in the photosynthetic reaction centers (RC) from purple bacterium Rhodobacter sphaeroides depends nonmonotonically on temperature. The time of this reaction is similar to100 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 Q(A)(-) 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.
- Добавил в систему: Красильников Павел Михайлович