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...

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Autores principales:	Ewald Weichselbaum, Maria Österbauer, Denis G. Knyazev, Oleg V. Batishchev, Sergey A. Akimov, Trung Hai Nguyen, Chao Zhang, Günther Knör, Noam Agmon, Paolo Carloni, Peter Pohl
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e79296c0e9db4ab09bce85c16733cc1a
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spelling	oai:doaj.org-article:e79296c0e9db4ab09bce85c16733cc1a2021-12-02T15:04:52ZOrigin of proton affinity to membrane/water interfaces10.1038/s41598-017-04675-92045-2322https://doaj.org/article/e79296c0e9db4ab09bce85c16733cc1a2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04675-9https://doaj.org/toc/2045-2322Abstract 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.Ewald WeichselbaumMaria ÖsterbauerDenis G. KnyazevOleg V. BatishchevSergey A. AkimovTrung Hai NguyenChao ZhangGünther KnörNoam AgmonPaolo CarloniPeter PohlNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ewald Weichselbaum Maria Österbauer Denis G. Knyazev Oleg V. Batishchev Sergey A. Akimov Trung Hai Nguyen Chao Zhang Günther Knör Noam Agmon Paolo Carloni Peter Pohl Origin of proton affinity to membrane/water interfaces
description	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.
format	article
author	Ewald Weichselbaum Maria Österbauer Denis G. Knyazev Oleg V. Batishchev Sergey A. Akimov Trung Hai Nguyen Chao Zhang Günther Knör Noam Agmon Paolo Carloni Peter Pohl
author_facet	Ewald Weichselbaum Maria Österbauer Denis G. Knyazev Oleg V. Batishchev Sergey A. Akimov Trung Hai Nguyen Chao Zhang Günther Knör Noam Agmon Paolo Carloni Peter Pohl
author_sort	Ewald Weichselbaum
title	Origin of proton affinity to membrane/water interfaces
title_short	Origin of proton affinity to membrane/water interfaces
title_full	Origin of proton affinity to membrane/water interfaces
title_fullStr	Origin of proton affinity to membrane/water interfaces
title_full_unstemmed	Origin of proton affinity to membrane/water interfaces
title_sort	origin of proton affinity to membrane/water interfaces
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/e79296c0e9db4ab09bce85c16733cc1a
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_version_	1718389050899955712

Origin of proton affinity to membrane/water interfaces

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