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000834626 245__ $$aOrigin of proton affinity to membrane/water interfaces
000834626 260__ $$aLondon$$bNature Publishing Group$$c2017
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000834626 520__ $$aProton diffusion along biological membranes is vitally important for cellular energetics. Here we extended previous time-resolved fluorescence measurements to study the time and temperature dependence of surface proton transport. We determined the Gibbs activation energy barrier ΔG‡r that opposes proton surface-to-bulk release from Arrhenius plots of (i) protons’ surface diffusion constant and (ii) the rate coefficient for proton surface-to-bulk release. The large size of ΔG‡r disproves that quasi-equilibrium exists in our experiments between protons in the near-membrane layers and in the aqueous bulk. Instead, non-equilibrium kinetics describes the proton travel between the site of its photo-release and its arrival at a distant membrane patch at different temperatures. ΔG‡r contains only a minor enthalpic contribution that roughly corresponds to the breakage of a single hydrogen bond. Thus, our experiments reveal an entropic trap that ensures channeling of highly mobile protons along the membrane interface in the absence of potent acceptors.
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000834626 7001_ $$0P:(DE-HGF)0$$aÖsterbauer, Maria$$b1
000834626 7001_ $$0P:(DE-HGF)0$$aKnyazev, Denis G.$$b2
000834626 7001_ $$0P:(DE-HGF)0$$aBatishchev, Oleg V.$$b3
000834626 7001_ $$aAkimov, Sergey A.$$b4
000834626 7001_ $$0P:(DE-HGF)0$$aHai Nguyen, Trung$$b5
000834626 7001_ $$0P:(DE-Juel1)136680$$aZhang, Chao$$b6
000834626 7001_ $$0P:(DE-HGF)0$$aKnör, Günther$$b7
000834626 7001_ $$0P:(DE-HGF)0$$aAgmon, Noam$$b8
000834626 7001_ $$0P:(DE-Juel1)145614$$aCarloni, Paolo$$b9$$ufzj
000834626 7001_ $$0P:(DE-HGF)0$$aPohl, Peter$$b10$$eCorresponding author
000834626 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/s41598-017-04675-9$$gVol. 7, no. 1, p. 4553$$n1$$p4553$$tScientific reports$$v7$$x2045-2322$$y2017
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