Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization.
Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization.
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DOI：
10.1063/1.4948338
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发表时间：
2016-07
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影响因子：
--
通讯作者：
Heyne K
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文献类型：
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作者：
Stensitzki T;Yang Y;Muders V;Schlesinger R;Heberle J;Heyne K
利用飞秒可见泵浦中红外探针光谱研究了奥古斯特衣藻（Chlamydomonas augustae, CaChR1）通道视紫红质-1视网膜全反式到13顺式光异构化的振动动力学。光激发后，检测了C-C拉伸模式的瞬态红外吸收。在0.3 ps的时间分辨率内，在1193 cm−1处观察到13顺式光产物标记带的形成。我们估计光异构化收率为（60±6）%。我们发现冷却和反反应冷却过程的额外时间常数分别为（0.55±0.05）ps和（6±1）ps。一个额外的漂白带显示视网膜的基态异质性。
Vibrational dynamics of the retinal all-trans to 13-cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected. The formation of the 13-cis photoproduct marker band at 1193 cm−1 was observed within the time resolution of 0.3 ps. We estimated the photoisomerization yield to (60 ± 6) %. We found additional time constants of (0.55 ± 0.05) ps and (6 ± 1) ps, assigned to cooling, and cooling processes with a back-reaction pathway. An additional bleaching band demonstrates the ground-state heterogeneity of retinal.