The Journal of General Physiology
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The Journal of General Physiology, Vol 41, 501-528, Copyright © 1958 by The Rockefeller University Press


ARTICLE

THE RHODOPSIN SYSTEM OF THE SQUID

Ruth Hubbard 1 and Robert C. C. St. George 1

1 From the Biological Laboratories of Harvard University, Cambridge

Squid rhodopsin (lambdamax 493 mµ)—like vertebrate rhodopsins—contains a retinene chromophore linked to a protein, opsin. Light transforms rhodopsin to lumi- and metarhodopsin. However, whereas vertebrate metarhodopsin at physiological temperatures decomposes into retinene and opsin, squid metarhodopsin is stable.

Light also converts squid metarhodopsin to rhodopsin. Rhodopsin is therefore regenerated from metarhodopsin in the light. Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions,

See PDF for Equation

Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene. The interconversion of rhodopsin and metarhodopsin involves only the stereoisomerization of their chromophores.

Squid metarhodopsin is a pH indicator, red (lambdamax 500 mµ) near neutrality, yellow (lambdamax 380 mµ) in alkaline solution. The two forms—acid and alkaline metarhodopsin—are interconverted according to the equation,

Alkaline metarhodopsin + H+ rlhar2acid metarhodopsin,

with pK 7.7. In both forms, retinene is attached to opsin at the same site as in rhodopsin. However, metarhodopsin decomposes more readily than rhodopsin into retinene and opsin.

The opsins apparently fit the shape of the neo-b chromophore. When light isomerizes the chromophore to the all-trans configuration, squid opsin accepts the all-trans chromophore, while vertebrate opsins do not and hence release all-trans retinene.

Light triggers vision by affecting directly the shape of the retinene chromophore. This changes its relationship with opsin, so initiating a train of chemical reactions.

Submitted on July 15, 1957


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