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Response of the water-protein media on the ion-radical pair formation in the rc of purple bacteriaстатья
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Авторы: Paschenko Vladimir Z., Knox Peter P., Rubin Andrew B.
- Журнал: European Biophysics Journal
- Том: 29
- Номер: 4-5
- Год издания: 2000
- Издательство: Springer Verlag
- Местоположение издательства: Germany
- Первая страница: 322
- Последняя страница: 322
- Аннотация: Cofactors of electron transfer in bacterial reaction centre are: a) dimer of bacteriochlorophyll molecules P~P2; b) monomeric molecules of bacteriochlorophyll (BC1) and bacteriopheophytin (BPh) and c) quinone acceptor QA. These cofactors are connected to the proteins by means of hydrogen bonds. After light excitation of a dimer P a charge transfer (CT) state {Pl^+ P2^-}* occures. As a result of the electron transfer (charge separation process) from this CT state to the BPh molecule the ion-radical pair P+BPh- is formed during ~3 ps. The next step is the electron transfer to quinone acceptor QA within ~200 ps. Nonequlibrium dipoles PI+P2-; P+BPh- and P+QA- relax to the pseudoequilibrium states as a result of solvation processes. In this study a dynamic of water-protein surrounding of cofactors caused by the formation of the electric dipole in RC is studied experimentally and analysed on the base of simple mechanical models. It is shown that the deformation of hydrogen bonds as a result of proton displacement in the electric field of central dipole (charge) takes place during ~100 fs. In this process the energy ~0.05 eV is stored. The results of this study are considered in the frame of the regulatory role of protein molecules in the charge separation and electron transfer reactions in photosynthesis.
- Добавил в систему: Пащенко Владимир Захарович