Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 60, Issue 30, Pages 16442-16447Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202015797
Keywords
channelrhodopsin; dynamic nuclear polarization; membrane proteins; photocycle; solid-state NMR spectroscopy
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Funding
- Deutsche Forschungsgemeinschaft [Sonderforschungsbereich 807]
- DFG [GL 307/4-1]
- State of Hesse
- Projekt DEAL
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Channelrhodopsin-2 (ChR2) is a light-gated cation channel used in optogenetics research. Despite the dark state structure being determined, the mechanistic understanding of channel function remains incomplete, requiring more detailed information on different photointermediates to be collected.
Channelrhodopsin-2 (ChR2) is a light-gated cation channel and was used to lay the foundations of optogenetics. Its dark state X-ray structure has been determined in 2017 for the wild-type, which is the prototype for all other ChR variants. However, the mechanistic understanding of the channel function is still incomplete in terms of structural changes after photon absorption by the retinal chromophore and in the framework of functional models. Hence, detailed information needs to be collected on the dark state as well as on the different photointermediates. For ChR2 detailed knowledge on the chromophore configuration in the different states is still missing and a consensus has not been achieved. Using DNP-enhanced solid-state MAS NMR spectroscopy on proteoliposome samples, we unambiguously determined the chromophore configuration in the desensitized state, and we show that this state occurs towards the end of the photocycle.
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