Journal Article

FZJ-2017-04534

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Origin of proton affinity to membrane/water interfaces

Weichselbaum, E. ; Österbauer, M. ; Knyazev, D. G. ; Batishchev, O. V. ; Akimov, S. A. ; Hai Nguyen, T. ; Zhang, C. ; Knör, G. ; Agmon, N. ; Carloni, P.FZJ* ; Pohl, P. (Corresponding author)

2017
Nature Publishing Group London

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Please use a persistent id in citations: http://hdl.handle.net/2128/14862  doi:10.1038/s41598-017-04675-9

Abstract: 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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Contributing Institute(s):

1. Computational Biomedicine (IAS-5)
2. Computational Biomedicine (INM-9)

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Appears in the scientific report 2017

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