The chromophore structure of the long-lived intermediate of the C128T channelrhodopsin-2 variant
The chromophore structure of the long-lived intermediate of the C128T channelrhodopsin-2 variant
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DOI:
10.1016/j.febslet.2011.11.007
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发表时间:
2011-12-15
期刊:
影响因子:
3.5
通讯作者:
Hildebrandt, Peter
中科院分区:
文献类型:
--
作者:
Bruun, Sara;Naumann, Hendrik;Hildebrandt, Peter
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.