A possible biological role of the electron transfer between tyrosine and tryptophan

FEBS Letters

Lee, Chyuan-Yih¹ 

[1] Chemical Dynamics Corporation, 204 Executive Drive, Guilderland, NY 12084, USA

关键词: Ion channel;    Electron transfer;    Tyrosine radical;    Tryptophan radical;   

DOI  :  10.1016/0014-5793(92)80228-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown