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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...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1958
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2194838/ https://www.ncbi.nlm.nih.gov/pubmed/13491819 |
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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 |
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