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The chromophore structure of the long-lived intermediate of the C128T channelrhodopsin-2 variant
Citation key Bruun2011
Author Bruun, Sara and Naumann, Hendrik and Kuhlmann, Uwe and Schulz, Claudia and Stehfest, Katja and Hegemann, Peter and Hildebrandt, Peter
Pages 3998–4001
Year 2011
DOI 10.1016/j.febslet.2011.11.007
Journal Febs Letters
Volume 585
Number 24
Abstract The photocycle of the light-activated channel, channelrhodopsin-2 C128T, has been studied by resonance Raman (RR) spectroscopy focussing on the intermediates P380 and P353 that constitute a side pathway in the recovery of the parent state. The P353 species displays a UV-vis absorption spectrum with a fine-structure reminiscent of the reduced-retro form of bacteriorhodopsin, whereas the respective RR spectra differ substantially. Instead, the RR spectra of the P380/P353 intermediate couple are closely related to that of a free retinal in the all-trans configuration. These findings imply that the parent state recovery via P380/P353 involves the transient hydrolysis and re-formation of the retinal-protein linkage. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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