Production of a Light-Gated Proton Channel by Replacing the Retinal Chromophore with Its Synthetic Vinylene Derivative

The Journal of Physical Chemistry Letters
Riho TakayamaYuki Sudo

Abstract

Rhodopsin is widely distributed in organisms as a membrane-embedded photoreceptor protein, consisting of the apoprotein opsin and vitamin-A aldehyde retinal, A1-retinal and A2-retinal being the natural chromophores. Modifications of opsin (e.g., by mutations) have provided insight into the molecular mechanism of the light-induced functions of rhodopsins as well as providing tools in chemical biology to control cellular activity by light. Instead of the apoprotein opsin, in this study, we focused on the retinal chromophore and synthesized three vinylene derivatives of A2-retinal. One of them, C(14)-vinylene A2-retinal (14V-A2), was successfully incorporated into the opsin of a light-driven proton pump archaerhodopsin-3 (AR3). Electrophysiological experiments revealed that the opsin of AR3 (archaeopsin3, AO3) with 14V-A2 functions as a light-gated proton channel. The engineered proton channel showed characteristic photochemical properties, which are significantly different from those of AR3. Thus, we successfully produced a proton channel by replacing the chromophore of AR3.

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Jan 1, 2015·Biophysics and Physicobiology·Marie Kurihara, Yuki Sudo

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Citations

Mar 13, 2019·Photochemistry and Photobiology·Srividya GanapathyWillem J de Grip
May 2, 2019·Nature Communications·Keiichi InoueHideki Kandori
Dec 10, 2019·Biochemistry·Keiichi KojimaYuki Sudo
Aug 29, 2018·Biochemistry·Yi-Chung ShenYasushi Imamoto

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