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- W89946977 abstract "Proton transfer to Qb proceeds in two steps, namely the proton delivery from the membrane surface to Qb is followed by the repletion of proton vacancies at the surface. The kinetics of proton transfer from the surface to Qb, as traced electrometrically in chromatophore vesicles, contained components with activation energy (Ea) of ~60 kJ/mol upon both semiquinone and quinol formation. Earlier we have putatively attributed these components to the twisting movement of the Qb ring between its two positions [1,2], which were revealed by X-ray crystallography [3,4]. In the mutants where Pro209 of the L-subunit of the RC was replaced by Tyr or Glu [5], the Ea value of these components of proton transfer was lower (~40 kJ/mol) than in the wild type. The steered molecular dynamics simulations showed that a smaller force, as compared to the wild type, was needed to cause a flip motion of the Qb ring between its two positions in the pocket of the mutant RC, in quantitative agreement with the difference in the Ea values of proton transfer. Hence, (i) Pro-L209 contributes to the tightness of the quinone-binding pocket and (ii) the high activation barrier for proton transfer seems to be coupled with the twisting relocation of the Qb ring." @default.
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- W89946977 date "2005-01-01" @default.
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