Abstract
The evolution of the light-induced absorption difference spectrum (380–500 nm) of the reaction centers from photosynthetic purple bacteria Rhodobacter sphaeroides has been examined over 200 μs. The observed changes are interpreted as the effects of proton movement along the H-bond between the primary quinone acceptor and its protein surroundings. A theoretical analysis of the spectral evolution, considering the proton tunneling kinetics, corroborates this interpretation. The electronic state of the primary quinone is stabilized within tens of microseconds; the process is retarded upon deuteration of the reaction center as well as in 90% glycerol, and accelerated upon nondestructive heating to 40°C.
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Original Russian Text © P.P. Knox, P.M. Krasilnikov, P.A. Mamonov, N.Kh. Seifullina, A.F. Uchoa, M.S. Baptista, 2008, published in Biofizika, 2008, Vol. 53, No. 4, pp. 624–631.
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Knox, P.P., Krasilnikov, P.M., Mamonov, P.A. et al. Stabilization of the electron in the quinone acceptor part of the Rhodobacter sphaeroides reaction centers. BIOPHYSICS 53, 291–295 (2008). https://doi.org/10.1134/S0006350908040106
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DOI: https://doi.org/10.1134/S0006350908040106