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Significance The Hv1 voltage-gated proton channels are important for various physiological functions that include the extrusion of acid from cells, oxidative bursts in phagocytes, and immune response. A lack of structural information under physiological conditions has left many unanswered questions about the mechanism of proton conduction. We employed molecular dynamics simulations to generate structural models of the open and closed states of the channel in the presence of applied membrane potentials, without any initial assumptions on the position of the voltage sensor and without relying on homology on functional similarities between Hv1 and other voltage-sensitive proteins. We have thus provided molecular-scale insights into the mechanism of voltage-dependent activation that could inform therapeutic strategies for modulating the function of Hv1.

Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations