Abstract
Significance: Voltage activation of proton transport is an important mechanism that plays a key role in fundamental biological processes, yet the detailed control of such processes is far from clear. Here we investigate the voltage-activated proton channel Hv1 to explore the structure/function basis of its activation by combining empirical valence bond and electrostatic calculations. Our study provides a detailed description of the exquisite use of an ionizable aspartic acid residue and arginine residues in controlling the crucial selectivity of the proton transport through the channel. This type of mechanism is likely to have implications for the action of other related systems.
Funding Information
  • HHS | National Institutes of Health (R35GM-122472)

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