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.
| Original language | English |
|---|---|
| Pages (from-to) | 2857-2862 |
| Number of pages | 6 |
| Journal | Journal of Physical Chemistry Letters |
| Volume | 9 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Jun 7 2018 |
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ASJC Scopus subject areas
- Materials Science(all)
Cite this
Production of a Light-Gated Proton Channel by Replacing the Retinal Chromophore with Its Synthetic Vinylene Derivative. / Takayama, Riho; Kaneko, Akimasa; Okitsu, Takashi; Tsunoda, Satoshi P.; Shimono, Kazumi; Mizuno, Misao; Kojima, Keiichi; Tsukamoto, Takashi; Kandori, Hideki; Mizutani, Yasuhisa; Wada, Akimori; Sudo, Yuki.
In: Journal of Physical Chemistry Letters, Vol. 9, No. 11, 07.06.2018, p. 2857-2862.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Production of a Light-Gated Proton Channel by Replacing the Retinal Chromophore with Its Synthetic Vinylene Derivative
AU - Takayama, Riho
AU - Kaneko, Akimasa
AU - Okitsu, Takashi
AU - Tsunoda, Satoshi P.
AU - Shimono, Kazumi
AU - Mizuno, Misao
AU - Kojima, Keiichi
AU - Tsukamoto, Takashi
AU - Kandori, Hideki
AU - Mizutani, Yasuhisa
AU - Wada, Akimori
AU - Sudo, Yuki
PY - 2018/6/7
Y1 - 2018/6/7
N2 - 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.
AB - 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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U2 - 10.1021/acs.jpclett.8b00879
DO - 10.1021/acs.jpclett.8b00879
M3 - Article
AN - SCOPUS:85047100186
VL - 9
SP - 2857
EP - 2862
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
SN - 1948-7185
IS - 11
ER -