Voltage gated proton channels (H V 1) are the most selective channels known, with no detectable permeability to any ion besides H þ . We recently identified the selectivity filter of the human voltage gated proton channel (hH V 1). Mutation of an aspartate residue, Asp 112 , in the middle of the S1 transmembrane domain resulted in loss of proton specificity. Surprisingly, mutant channels were anion selective. Cation substitution did not affect V rev at all. Replacing CH 3 SO 3 by Clshifted V rev negatively, showing that that Clis more permeable than CH 3 SO 3 -
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