期刊
FEBS LETTERS
卷 583, 期 22, 页码 3676-3680出版社
WILEY
DOI: 10.1016/j.febslet.2009.10.052
关键词
Bacteriorhodopsin; Proton transfer; Vibrational spectroscopy; Microbial rhodopsin; Light adaptation
资金
- Deutsche Forschungsgemeinschaft [SFB 613, K8, SFB 472, 807]
Channelrhodopsin-2 mediates phototaxis in green algae by acting as a light-gated cation channel. As a result of this property, it is used as a novel optogenetic tool in neurophysiological applications. Structural information is still scant and we present here the first resonance Raman spectra of channelrhodopsin-2. Spectra of detergent solubilized and lipid-reconstituted protein were recorded under pre-resonant conditions to exclusively probe retinal in its electronic ground state. All-trans retinal was identified to be the favoured configuration of the chromophore but significant contributions of 13-cis were detected. Pre-illumination hardly changed the isomeric composition but small amounts of presumably 9-cis retinal were found in the light-adapted state. Spectral analysis suggested that the Schiff base proton is strongly hydrogen-bonded to a nearby water molecule. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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