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

Nack M, Radu I, Bamann C, Bamberg E, Heberle J (2009)
FEBS Letters 583(22): 3676-3680.

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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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Nack M, Radu I, Bamann C, Bamberg E, Heberle J. The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy. FEBS Letters. 2009;583(22):3676-3680.
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
Nack, M., Radu, I., Bamann, C., Bamberg, E., and Heberle, J. (2009). The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy. FEBS Letters 583, 3676-3680.
Nack, M., et al., 2009. The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy. FEBS Letters, 583(22), p 3676-3680.
M. Nack, et al., “The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy”, FEBS Letters, vol. 583, 2009, pp. 3676-3680.
Nack, M., Radu, I., Bamann, C., Bamberg, E., Heberle, J.: The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy. FEBS Letters. 583, 3676-3680 (2009).
Nack, Melanie, Radu, Ionela, Bamann, Christian, Bamberg, Ernst, and Heberle, Joachim. “The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy”. FEBS Letters 583.22 (2009): 3676-3680.
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28 Citations in Europe PMC

Data provided by Europe PubMed Central.

The DC gate in Channelrhodopsin-2: crucial hydrogen bonding interaction between C128 and D156.
Nack M, Radu I, Gossing M, Bamann C, Bamberg E, von Mollard GF, Heberle J., Photochem Photobiol Sci 9(2), 2010
PMID: 20126794
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Stehfest K, Hegemann P., Chemphyschem 11(6), 2010
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The photocycle of channelrhodopsin-2: ultrafast reaction dynamics and subsequent reaction steps.
Verhoefen MK, Bamann C, Blöcher R, Förster U, Bamberg E, Wachtveitl J., Chemphyschem 11(14), 2010
PMID: 20730849

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