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245 _ _ |a Origin of proton affinity to membrane/water interfaces
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520 _ _ |a Proton diffusion along biological membranes is vitally important for cellular energetics. Here we extended previous time-resolved fluorescence measurements to study the time and temperature dependence of surface proton transport. We determined the Gibbs activation energy barrier ΔG‡r that opposes proton surface-to-bulk release from Arrhenius plots of (i) protons’ surface diffusion constant and (ii) the rate coefficient for proton surface-to-bulk release. The large size of ΔG‡r disproves that quasi-equilibrium exists in our experiments between protons in the near-membrane layers and in the aqueous bulk. Instead, non-equilibrium kinetics describes the proton travel between the site of its photo-release and its arrival at a distant membrane patch at different temperatures. ΔG‡r contains only a minor enthalpic contribution that roughly corresponds to the breakage of a single hydrogen bond. Thus, our experiments reveal an entropic trap that ensures channeling of highly mobile protons along the membrane interface in the absence of potent acceptors.
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700 1 _ |a Österbauer, Maria
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700 1 _ |a Knyazev, Denis G.
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700 1 _ |a Batishchev, Oleg V.
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700 1 _ |a Akimov, Sergey A.
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700 1 _ |a Hai Nguyen, Trung
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700 1 _ |a Zhang, Chao
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700 1 _ |a Knör, Günther
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700 1 _ |a Agmon, Noam
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700 1 _ |a Carloni, Paolo
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700 1 _ |a Pohl, Peter
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