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| 024 | 7 | _ | |a 10.1038/s41598-017-04675-9 |2 doi |
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| 245 | _ | _ | |a Origin of proton affinity to membrane/water interfaces |
| 260 | _ | _ | |a London |c 2017 |b Nature Publishing Group |
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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 |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Knyazev, Denis G. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Batishchev, Oleg V. |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Akimov, Sergey A. |b 4 |
| 700 | 1 | _ | |a Hai Nguyen, Trung |0 P:(DE-HGF)0 |b 5 |
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| 700 | 1 | _ | |a Knör, Günther |0 P:(DE-HGF)0 |b 7 |
| 700 | 1 | _ | |a Agmon, Noam |0 P:(DE-HGF)0 |b 8 |
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| 700 | 1 | _ | |a Pohl, Peter |0 P:(DE-HGF)0 |b 10 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s41598-017-04675-9 |g Vol. 7, no. 1, p. 4553 |0 PERI:(DE-600)2615211-3 |n 1 |p 4553 |t Scientific reports |v 7 |y 2017 |x 2045-2322 |
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