Abstract
The biophysical properties of the voltage gated proton channel (H(V)1) are the key elements of its physiological function. The voltage gated proton channel is a unique molecule that in contrast to all other ion channels is exclusively selective for protons. Alone among proton channels, it has voltage and time dependent gating like other "classical" ion channels. H(V)1 is furthermore a sensor for the pH in the cell and the surrounding media. Its voltage dependence is strictly coupled to the pH gradient across the membrane. This regulation restricts opening of the channel to specific voltages at any given pH gradient, therefore allowing H(V)1 to perform its physiological task in the tissue it is expressed in. For H(V)1 there is no known blocker. The most potent channel inhibitor is zinc (Zn(2+)) which prevents channel opening. An additional characteristic of H(V)1 is its strong temperature dependence of both gating and conductance. In contrast to single-file water filled pores like the gramicidin channel, H(V)1 exhibits pronounced deuterium effects and temperature effects on conduction, consistent with a different conduction mechanism than other ion channels. These properties may be explained by the recent identification of an aspartate in the pore of H(V)1 that is essential to its proton selectivity.