all-trans-retinal forms a visible-absorbing pigment with human rod opsin

Citation
Li. Brueggemann et Jm. Sullivan, all-trans-retinal forms a visible-absorbing pigment with human rod opsin, BIOCHEM, 40(14), 2001, pp. 4446-4453
Citations number
41
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMISTRY
ISSN journal
00062960 → ACNP
Volume
40
Issue
14
Year of publication
2001
Pages
4446 - 4453
Database
ISI
SICI code
0006-2960(20010410)40:14<4446:AFAVPW>2.0.ZU;2-Q
Abstract
Rhodopsin activation elicits transmembrane currents due to electrostatic ev ents associated with conformational changes. We employed the sensitive rhod opsin early receptor current approach to reevaluate whether all-trans-retin al can form a visual pigment with rod opsin apoprotein. An opsin shift abov e 440 nm is induced in the action spectrum of charge motions caused by visi ble flashes in cells expressing human rod opsin and regenerated with all-tr ans-retinal, compared to cells without opsin. Near-ultraviolet stimulation of opsin regenerated with all-trans-retinal promotes charge motions similar to those arising from the meta-II signaling state while photochemically re generating a pigment with ground state charge motion properties. These resu lts indicate that all-trans-retinal can form a visual pigment with opsin, t hrough both protonated and unprotonated Schiff base linkages and likely wit hin the native ligand binding pocket at lysine-296. The agonist effects of all-trans-retinal may relate to its structural accommodation within the cor e of opsin, similar to other G-protein-coupled receptors.