Origin of proton affinity to membrane/water interfaces.

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

SUBMITTER: Weichselbaum E 

PROVIDER: S-EPMC5495794 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature