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Journal Article

The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy

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Bamann,  Christian
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Nack, M., Radu, I., Bamann, C., Bamberg, E., & Heberle, J. (2009). The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy. FEBS Letters, 583(22), 3676-3680. doi:10.1016/j.febslet.2009.10.052.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D7B9-7
Abstract
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.