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The chromophore structure of the long-lived intermediate of the C128T channelrhodopsin-2 variant
Zitatschlüssel Bruun2011
Autor Bruun, Sara and Naumann, Hendrik and Kuhlmann, Uwe and Schulz, Claudia and Stehfest, Katja and Hegemann, Peter and Hildebrandt, Peter
Seiten 3998–4001
Jahr 2011
DOI 10.1016/j.febslet.2011.11.007
Journal Febs Letters
Jahrgang 585
Nummer 24
Zusammenfassung 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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