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Structure of the chromophoric group in bathorhodopsin

Authors :
FRANSEN, M. R.
LUYTEN, W. C. M. M.
VAN THUIJL, J.
LUGTENBURG, J.
JANSEN, P. A. A.
VAN BREUGEL, P. J. G. M.
DAEMEN, F. J. M.
Source :
Nature; April 1976, Vol. 260 Issue: 5553 p726-727, 2p
Publication Year :
1976

Abstract

IN the photolysis of the visual pigment rhodopsin the intermediate first observed is bathorhodopsin1,2(formerly called prelumirhodopsin). It is generally held that isomerisation of 11-cis to all-trans retinal occurs during this initial step. On theoretical grounds, however, an hexaene–amine structure (Fig. 1) has been proposed as an alternative for the chromophore of bathorodopsin (ref. 3 and unpublished results of K. Van der Meer, J. J. C. Mulder and J.L.). This chromophore has an exomethylene double bond between the atoms C5 and C18 and the nitrogen of its ene–amine moiety derives from the ɛ-amino group of a lysine residue of opsin. It is a retrotautomer of the chromophoric group in native rhodopsin which is a protonated Schiff base of 11-cis retinal. We now present two lines of evidence which support the structure depicted in Fig. 1: first, the interpretation of a recently published laser resonance Raman spectrum of bathorhodopsin4, and second, experiments which establish hydrogen (deuterium) exchange during photolysis of rhodopsin.

Details

Language :
English
ISSN :
00280836 and 14764687
Volume :
260
Issue :
5553
Database :
Supplemental Index
Journal :
Nature
Publication Type :
Periodical
Accession number :
ejs25222862
Full Text :
https://doi.org/10.1038/260726a0