Abstract:
:Halorhodopsin (HR) and sensory rhodopsin (SR) have been regenerated with retinal analogues that are covalently locked in the 6-s-cis or 6-s-trans conformations. Both pigments regenerate more completely with the locked 6-s-trans retinal and produce analogue pigments with absorption maxima (577 nm for HR and 592 nm for SR) nearly identical to those of the native pigments (577 and 587 nm). This indicates that HR and SR bind retinal in the 6-s-trans conformation. The opsin shift for the locked 6-s-trans analogue in HR is 1,200 cm-1 less than that for the native chromophore (5,400 cm-1). The opsin shift for the 6-s-trans analogue in SR is 1,100 cm-1 less than that for the native retinal (5,700 cm-1). This demonstrates that approximately 20% of the opsin shift in these pigments arises from a protein-induced change in the chromophore conformation from twisted 6-s-cis in solution to planar 6-s-trans in the protein. The reduced opsin shift observed for the locked 6-s-cis analogue pigments compared with the locked 6-s-trans pigments may be due to a positive electrostatic perturbation near C7.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Baselt DR,Fodor SP,van der Steen R,Lugtenburg J,Bogomolni RA,Mathies RAdoi
10.1016/S0006-3495(89)82791-2subject
Has Abstractpub_date
1989-01-01 00:00:00pages
193-6issue
1eissn
0006-3495issn
1542-0086pii
S0006-3495(89)82791-2journal_volume
55pub_type
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