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Water at hydrophobic interfaces delays proton surface-to-bulk transfer and provides a pathway for lateral proton diffusion.

Abstract：

:Fast lateral proton migration along membranes is of vital importance for cellular energy homeostasis and various proton-coupled transport processes. It can only occur if attractive forces keep the proton at the interface. How to reconcile this high affinity to the membrane surface with high proton mobility is unclear. Here, we tested whether a minimalistic model interface between an apolar hydrophobic phase (n-decane) and an aqueous phase mimics the biological pathway for lateral proton migration. The observed diffusion span, on the order of tens of micrometers, and the high proton mobility were both similar to the values previously reported for lipid bilayers. Extensive ab initio simulations on the same water/n-decane interface reproduced the experimentally derived free energy barrier for the excess proton. The free energy profile G(H(+)) adopts the shape of a well at the interface, having a width of two water molecules and a depth of 6 ± 2RT. The hydroniums in direct contact with n-decane have a reduced mobility. However, the hydroniums in the second layer of water molecules are mobile. Their in silico diffusion coefficient matches that derived from our in vitro experiments, (5.7 ± 0.7) 10(-5) cm(2) s(-1). Conceivably, these are the protons that allow for fast diffusion along biological membranes.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Zhang C,Knyazev DG,Vereshaga YA,Ippoliti E,Nguyen TH,Carloni P,Pohl P

doi

10.1073/pnas.1121227109

subject

Has Abstract

pub_date

2012-06-19 00:00:00

pages

9744-9

issue

25

eissn

0027-8424

issn

1091-6490

pii

1121227109

journal_volume

109

pub_type

杂志文章

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