Light-Induced Charge Redistribution in the Retinal Chromophore Is Required for Initiating the Bacteriorhodopsin Photocycle
Bacteriorhodopsin's photocycle is initiated by the retinal chromophore light absorption. It has usually been assumed that light primarily isomerizes a retinal double bond which in turn induces protein conformational alterations and biological activity. We have studied several artificial pigment...
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| Veröffentlicht in: | Journal of the American Chemical Society 2002-10, Vol.124 (40), p.11844-11845 |
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| container_issue | 40 |
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| container_title | Journal of the American Chemical Society |
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| creator | Zadok, Uri Khatchatouriants, Artium Lewis, Aaron Ottolenghi, Michael Sheves, Mordechai |
| description | Bacteriorhodopsin's photocycle is initiated by the retinal chromophore light absorption. It has usually been assumed that light primarily isomerizes a retinal double bond which in turn induces protein conformational alterations and biological activity. We have studied several artificial pigments derived from retinal analogues tailored to substantially reduce the light-induced chromophore polarization. The lack of chromophore polarization was reflected in an undetectable second harmonic generation (SHG) signal. It was revealed that these artificial pigments did not exhibit any detectable light-induced photocycle nor light acceleration of the hydroxylamine-bleaching reaction. We suggest that light-induced retinal polarization triggers protein polarization which controls the course of the isomerization reaction by determining the relative efficiency of forward versus back-branching processes. |
| doi_str_mv | 10.1021/ja0274251 |
| format | Article |
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It has usually been assumed that light primarily isomerizes a retinal double bond which in turn induces protein conformational alterations and biological activity. We have studied several artificial pigments derived from retinal analogues tailored to substantially reduce the light-induced chromophore polarization. The lack of chromophore polarization was reflected in an undetectable second harmonic generation (SHG) signal. It was revealed that these artificial pigments did not exhibit any detectable light-induced photocycle nor light acceleration of the hydroxylamine-bleaching reaction. 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Am. Chem. Soc</addtitle><description>Bacteriorhodopsin's photocycle is initiated by the retinal chromophore light absorption. It has usually been assumed that light primarily isomerizes a retinal double bond which in turn induces protein conformational alterations and biological activity. We have studied several artificial pigments derived from retinal analogues tailored to substantially reduce the light-induced chromophore polarization. The lack of chromophore polarization was reflected in an undetectable second harmonic generation (SHG) signal. It was revealed that these artificial pigments did not exhibit any detectable light-induced photocycle nor light acceleration of the hydroxylamine-bleaching reaction. We suggest that light-induced retinal polarization triggers protein polarization which controls the course of the isomerization reaction by determining the relative efficiency of forward versus back-branching processes.</description><subject>Analytical biochemistry: general aspects, technics, instrumentation</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacteriorhodopsins - chemistry</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isomerism</subject><subject>Light</subject><subject>Molecular Conformation</subject><subject>Photochemistry</subject><subject>Pigments, Biological - chemistry</subject><subject>Retinaldehyde - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0ctuGyEUBmBUtWqctIu-QDWbVspiUjjcJsvG6sWRpaSNu0YMAx7c8eAAIzV9-pLaijdZIeA7v9APQu8IviAYyKeNxiAZcPICzQgHXHMC4iWaYYyhlo2gJ-g0pU3ZMmjIa3RCgPKGEzFDf5d-3ed6MXaTsV0173Vc2-qn7XzK0bdT9mGs_Fjl_vE0-1EPBcWwDbs-RFstUjm-n3wswy7EajH67HVx6_8jV9pkG32IfejCLpWg2z7kYB7MYN-gV04Pyb49rGfo19cvq_n3ennzbTH_vKw1YzzXAhwD2YJuOnC0tS0TVLQgHDCnW-0IY50TxkAHABxLblspBZCuCEqto2fo4z53F8P9ZFNWW5-MHQY92jAlJYEwTiUr8HwPTQwpRevULvqtjg-KYPVYtHoqutj3h9Cp3druKA_NFvDhAHQyenBRj8ano6OXgtJLKK7eu1K4_fN0r-NvJSSVXK1u79Qdvl42K_ih-DFXm6Q2YYrlR9IzD_wHT_Ohpg</recordid><startdate>20021009</startdate><enddate>20021009</enddate><creator>Zadok, Uri</creator><creator>Khatchatouriants, Artium</creator><creator>Lewis, Aaron</creator><creator>Ottolenghi, Michael</creator><creator>Sheves, Mordechai</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20021009</creationdate><title>Light-Induced Charge Redistribution in the Retinal Chromophore Is Required for Initiating the Bacteriorhodopsin Photocycle</title><author>Zadok, Uri ; Khatchatouriants, Artium ; Lewis, Aaron ; Ottolenghi, Michael ; Sheves, Mordechai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-62f427b2a8d2f3beb4636b26f24fabaf144df6cc2d2225075eb77621d6f233ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Analytical biochemistry: general aspects, technics, instrumentation</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacteriorhodopsins - chemistry</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Isomerism</topic><topic>Light</topic><topic>Molecular Conformation</topic><topic>Photochemistry</topic><topic>Pigments, Biological - chemistry</topic><topic>Retinaldehyde - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zadok, Uri</creatorcontrib><creatorcontrib>Khatchatouriants, Artium</creatorcontrib><creatorcontrib>Lewis, Aaron</creatorcontrib><creatorcontrib>Ottolenghi, Michael</creatorcontrib><creatorcontrib>Sheves, Mordechai</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zadok, Uri</au><au>Khatchatouriants, Artium</au><au>Lewis, Aaron</au><au>Ottolenghi, Michael</au><au>Sheves, Mordechai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Light-Induced Charge Redistribution in the Retinal Chromophore Is Required for Initiating the Bacteriorhodopsin Photocycle</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2002-10-09</date><risdate>2002</risdate><volume>124</volume><issue>40</issue><spage>11844</spage><epage>11845</epage><pages>11844-11845</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>Bacteriorhodopsin's photocycle is initiated by the retinal chromophore light absorption. It has usually been assumed that light primarily isomerizes a retinal double bond which in turn induces protein conformational alterations and biological activity. We have studied several artificial pigments derived from retinal analogues tailored to substantially reduce the light-induced chromophore polarization. The lack of chromophore polarization was reflected in an undetectable second harmonic generation (SHG) signal. It was revealed that these artificial pigments did not exhibit any detectable light-induced photocycle nor light acceleration of the hydroxylamine-bleaching reaction. We suggest that light-induced retinal polarization triggers protein polarization which controls the course of the isomerization reaction by determining the relative efficiency of forward versus back-branching processes.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12358516</pmid><doi>10.1021/ja0274251</doi><tpages>2</tpages></addata></record> |
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| ispartof | Journal of the American Chemical Society, 2002-10, Vol.124 (40), p.11844-11845 |
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| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | Analytical biochemistry: general aspects, technics, instrumentation Analytical, structural and metabolic biochemistry Bacteriorhodopsins - chemistry Biological and medical sciences Fundamental and applied biological sciences. Psychology Isomerism Light Molecular Conformation Photochemistry Pigments, Biological - chemistry Retinaldehyde - chemistry |
| title | Light-Induced Charge Redistribution in the Retinal Chromophore Is Required for Initiating the Bacteriorhodopsin Photocycle |
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