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Tautomeric Forms of Metarhodopsin

The Journal of General Physiology · 1963 · Vol. 47(2) · pp. 215–240
Rowena G. MatthewsRuth HubbardPaul K. BrownGeorge Wald

Abstract

Light isomerizes the chromophore of rhodopsin, 11-cis retinal (formerly retinene), to the all-trans configuration. This introduces a succession of unstable intermediates-pre-lumirhodopsin, lumirhodopsin, metarhodopsin -in which all-trans retinal is still attached to the chromophoric site on opsin. Finally, retinal is hydrolyzed from opsin. The present experiments show that metarhodopsin exists in two tautomeric forms, metarhodopsins I and II, with lambda(max) 478 and 380 mmicro. Metarhodopsin I appears first, then enters into equilibrium with metarhodopsin II. In this equilibrium, the proportion of metarhodopsin II is favored by higher temperature or pH, neutral salts, and glycerol. The change from metarhodopsin I to II involves the binding of a proton by a group with pK 6.4 (imidazole?), and a large increase of entropy. Metarhodopsin II has been confused earlier with the final mixture of all-trans retinal and opsin (lambda(max) 387 mmicro), which it resembles in spectrum. These two products are, however, readily distinguished experimentally.

Photoreceptor and optogenetics researchRetinal Development and DisordersNeuroscience and Neuropharmacology ResearchOpsinRhodopsinRetinalChromophoreChemistryTautomerRetinaldehydeStereochemistryPhotochemistryBiochemistry

MeSH terms

AnimalsAnuraCattleChemistryEquipment and SuppliesGlycerolHydrogen-Ion ConcentrationLightMolluscaProtonsRetinaRetinal PigmentsRetinaldehydeRhodopsinTemperature
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