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A possible biological role of the electron transfer between tyrosine and tryptophan
Author(s) -
Lee Chyuan-Yih
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80228-9
Subject(s) - tryptophan , tyrosine , electron transfer , chemistry , biophysics , tetrodotoxin , hydrogen bond , stereochemistry , photochemistry , biochemistry , amino acid , molecule , biology , organic chemistry
Experiments have demonstrated that four tryptophan residues are located near the tetrodotoxin binding site in Na + channels, and that conserved tyrosine and tryptophan residues are located in the pore‐forming region of voltage‐sensitive K + channels. This paper proposes an activation mechanism involving electron transfer between these residues. The K + channel may be closed by four tyrosine residues forming hydrogen bonds with each other. After electron transfer, these hydrogen bonds will be broken, thereby opening the channel. The Na + channel could be activated by a similar mechanism. This idea can be tested directly by observing tyrosine or tryptophan radicals when the channels are in the open state.