Abstract. Voltage-gated proton selective channels occupy an ill-defined region between "normal" ion channels and a variety of proton-conducting pathways inside proteins, including, but not limited to, membrane-bound proteins. Voltage-gated H+ channels closely resemble other voltage-gated ion channels in their voltage-and time-dependent gating, but differ in their extreme selectivity, their miniscule singlechannel conductance, and the high activation enthalpy for conduction. Furthermore, in contrast with the "multiple occupancy" hypothesized to account for aspects of permeation through other ion channels, it seems unlikely that H' channels can be occupied by more than one proton at a time. Voltage-gated H+ channels functionally resemble other proton-conducting pathways in proteins, but until their structure has been determined, this similarity will remain speculative. The present restriction to functional measurements is less of a handicap than might be expected-the history of ion channel research shows that deductions based on electrophysiological measurements often closely predict the eventually determined structure. Existing evidence supports the idea that protons permeate the membrane through voltage-gated H+ channels by hopping across a hydrogen-bonded chain that consists of at least some amino acid side groups in addition to water molecules.