Cargando…

THE RHODOPSIN SYSTEM OF THE SQUID

Squid rhodopsin (λ(max) 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 metarhodopsi...

Descripción completa

Detalles Bibliográficos
Autores principales: Hubbard, Ruth, St. George, Robert C. C.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1958
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2194838/
https://www.ncbi.nlm.nih.gov/pubmed/13491819
_version_ 1782147704943542272
author Hubbard, Ruth
St. George, Robert C. C.
author_facet Hubbard, Ruth
St. George, Robert C. C.
author_sort Hubbard, Ruth
collection PubMed
description Squid rhodopsin (λ(max) 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 (λ(max) 500 mµ) near neutrality, yellow (λ(max) 380 mµ) in alkaline solution. The two forms—acid and alkaline metarhodopsin—are interconverted according to the equation, Alkaline metarhodopsin + H(+) ⇌acid 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.
format Text
id pubmed-2194838
institution National Center for Biotechnology Information
language English
publishDate 1958
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21948382008-04-23 THE RHODOPSIN SYSTEM OF THE SQUID Hubbard, Ruth St. George, Robert C. C. J Gen Physiol Article Squid rhodopsin (λ(max) 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 (λ(max) 500 mµ) near neutrality, yellow (λ(max) 380 mµ) in alkaline solution. The two forms—acid and alkaline metarhodopsin—are interconverted according to the equation, Alkaline metarhodopsin + H(+) ⇌acid 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. The Rockefeller University Press 1958-01-20 /pmc/articles/PMC2194838/ /pubmed/13491819 Text en Copyright © Copyright, 1958, by The Rockefeller Institute for Medical Research This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Hubbard, Ruth
St. George, Robert C. C.
THE RHODOPSIN SYSTEM OF THE SQUID
title THE RHODOPSIN SYSTEM OF THE SQUID
title_full THE RHODOPSIN SYSTEM OF THE SQUID
title_fullStr THE RHODOPSIN SYSTEM OF THE SQUID
title_full_unstemmed THE RHODOPSIN SYSTEM OF THE SQUID
title_short THE RHODOPSIN SYSTEM OF THE SQUID
title_sort rhodopsin system of the squid
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2194838/
https://www.ncbi.nlm.nih.gov/pubmed/13491819
work_keys_str_mv AT hubbardruth therhodopsinsystemofthesquid
AT stgeorgerobertcc therhodopsinsystemofthesquid
AT hubbardruth rhodopsinsystemofthesquid
AT stgeorgerobertcc rhodopsinsystemofthesquid