Effect of replacing the primary quinone by different species on the ultrafast photosynthetic electron transfer in bacterial reaction centresстатья

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[1] Effect of replacing the primary quinone by different species on the ultrafast photosynthetic electron transfer in bacterial reaction centres / S. L. Logunov, P. P. Knox, N. I. Zakharova et al. // Journal of Photochemistry and Photobiology B: Biology. — 1990. — Vol. 5, no. 1. — P. 41–47. Using picosecond absorption spectroscopy it has been shown that in Rhodobacter sphaeroides reaction centres the substitution of the primary quinone acceptor (QA), ubiquinone-10, by other quinone species (with redox potentials higher or lower than that of ubiquinone-10) has essentially no modifying effect on the reaction centre protein. The molecular relaxation processes that accompany the localization and stabilization of a photoexcited electron on the intermediate acceptor, bacteriopheophytin (I), are not affected, although the subsequent transfer of the electron from I to QA is slowed down. Consequently, this leads to a lower quantum efficiency of charge separation between the photoactive pigment and QA. Therefore the high rate of direct I− → QA reaction is normally due to the specificity of the primary quinone species and its binding site in the reaction centre protein which provide optimum steric and chemical conditions for an effective interaction between I and QA. [ DOI ]

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