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Resonance Raman study of intermediates of the halorhodopsin photocycle
Author(s) -
Diller R.,
Stockburger M.,
Oesterhelt D.,
Tittor J.
Publication year - 1987
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 - 10.1016/0014-5793(87)80682-8
Subject(s) - halorhodopsin , bacteriorhodopsin , deprotonation , schiff base , raman spectroscopy , halobacteriaceae , protonation , chemistry , resonance (particle physics) , photochemistry , base (topology) , resonance raman spectroscopy , stereochemistry , crystallography , biochemistry , halobacterium salinarum , membrane , organic chemistry , physics , ion , optics , mathematical analysis , mathematics , particle physics
The resonance Raman (RR) study of the retinal protein halorhodopsin (HR 578 ) was extended to two of its photoproducts: HR and HR L 410 RR spectra of both species were recorded in H 2 O and D 2 O and compared with the RR spectra of the intermediates L 550 and M 412 from the bacteriorhodopsin photocycle. HR 520 was found to be a protonated Schiff base in the 13‐ cis configuration and HR L 410 a deprotonated Schiff base in the 13‐ cis configuration.