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The chromophore structure of the long‐lived intermediate of the C128T channelrhodopsin‐2 variant
Author(s) -
Bruun Sara,
Naumann Hendrik,
Kuhlmann Uwe,
Schulz Claudia,
Stehfest Katja,
Hegemann Peter,
Hildebrandt Peter
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.11.007
Subject(s) - bacteriorhodopsin , resonance raman spectroscopy , chromophore , channelrhodopsin , chemistry , photochemistry , raman spectroscopy , absorption spectroscopy , crystallography , stereochemistry , optogenetics , biochemistry , biology , optics , physics , neuroscience , membrane
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.
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