Abstract
The light-gated dimeric cation channel channelrhodopsin-2 (ChR2) is one of the most important optogenetic tools. Upon light activation ChR2 undergoes conformational changes, the most prominent ones include a movement of transmembrane helix B. In the present work, we apply time resolved continuous wave EPR spectroscopy to follow spectral changes of a spin label bound to position C79 located in helix B. We observed an increase of the motional freedom of the spin label side chain in illuminated ChR2. The recovery of the underlying light-induced conformational change in the dark is correlated with the recovery of the P480 state of ChR2. The observed conformational changes might be thus key elements responsible for desensitizing the channel for cation conduction.
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