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| 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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