We report pH-dependent electrochemical rectification in a protein ion channel (the bacterial porin OmpF) reconstituted on a planar phospholipid membrane. The measurements performed at single-channel level show that the electric current is controlled by the protein fixed charge and it can be tuned by adjusting the local pH. Under highly asymmetric pH conditions, the channel behaves like a liquid diode. Unlike other nanofluidic devices that display also asymmetric conductance, here the microscopic charge distribution of the system can be explored by using the available high-resolution (2.4 A) channel crystallographic structure. Continuum electrostatics calculations confirm the hypothesized bipolar structure of the system. The selective titration of the channel residues is identified as the underlying physicochemical mechanism responsible for current rectification.

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Water molecules in confined geometries like nanopores and biological ion channels exhibit structural and dynamical properties very different from those found in free solution. Protein channels that open aqueous pores through biological membranes provide a complex spatial and electrostatic environment that decreases the translational and rotational mobility of water molecules, thus altering the effective dielectric constant of the pore water. By using the Booth equation, we study the effect of the large electric field created by ionizable residues of an hour-glass shaped channel, the bacterial porin OmpF, on the pore water dielectric constant, e w . We find a space-dependent significant reduction (down to 20) of e w that may explain some ad hoc assumptions about the dielectric constant of the protein and the water pore made to reconcile model calculations with measurements of permeation properties and pK a 's of protein residues. The electric potential calculations based on the OmpF protein atomic structure and the Booth field-dependent dielectric constant show that protein dielectric constants ca. 10 yield good agreement with molecular dynamics simulations as well as permeation experiments.

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