Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin
Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential t...
Gespeichert in:
| Veröffentlicht in: | arXiv.org 2019-05 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | |
| container_start_page | |
| container_title | arXiv.org |
| container_volume | |
| creator | Gabriela Nass Kovacs Jacques-Philippe Colletier Grünbein, Marie Yang, Yang Stensitzki, Till Batyuk, Alexander Carbajo, Sergio Doak, R Ehrenberg, David Foucar, Lutz Gasper, Raphael Alexander Gorel Hilpert, Mario Kloos, Marco Koglin, Jason Reinstein, Jochen Roome, Christopher Schlesinger, Ramona Seaberg, Matthew Shoeman, Robert Stricker, Miriam Boutet, Sébastien Haacke, Stefan Heberle, Joachim Heyne, Karsten Domratcheva, Tatiana Barends, Thomas Schlichting, Ilme |
| description | Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multi-photon effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins. |
| doi_str_mv | 10.48550/arxiv.1905.09002 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_arxiv</sourceid><recordid>TN_cdi_arxiv_primary_1905_09002</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2229498903</sourcerecordid><originalsourceid>FETCH-LOGICAL-a523-5189144f81f1ee8b6181e05c913f68ffb0fc21bcdae3920553f79b581fdb806a3</originalsourceid><addsrcrecordid>eNotj8tqwzAUREWh0JDmA7qqoGu7eliOtCyhj0BoN94bWb7CCrblSkqa_H3dpKuB4TDMQeiBkryQQpBnHU7umFNFRE4UIewGLRjnNJMFY3doFeOezG25ZkLwBfqsugCQtW6AMTo_6h4fHfxgb_GhT0FbHRNuz6MenInYjXjqfPJwMi5BixttEgTnQ-dbP0U33qNbq_sIq_9courttdp8ZLuv9-3mZZdpwXgmqFS0KKyklgLIpqSSAhFGUW5LaW1DrGG0Ma0GrhiZj9q1asSMt40kpeZL9HidvcjWU3CDDuf6T7q-SM_E05WYgv8-QEz13h_CrBdrxpgqlFSE8191VVsU</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2229498903</pqid></control><display><type>article</type><title>Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin</title><source>arXiv.org</source><source>Free E- Journals</source><creator>Gabriela Nass Kovacs ; Jacques-Philippe Colletier ; Grünbein, Marie ; Yang, Yang ; Stensitzki, Till ; Batyuk, Alexander ; Carbajo, Sergio ; Doak, R ; Ehrenberg, David ; Foucar, Lutz ; Gasper, Raphael ; Alexander Gorel ; Hilpert, Mario ; Kloos, Marco ; Koglin, Jason ; Reinstein, Jochen ; Roome, Christopher ; Schlesinger, Ramona ; Seaberg, Matthew ; Shoeman, Robert ; Stricker, Miriam ; Boutet, Sébastien ; Haacke, Stefan ; Heberle, Joachim ; Heyne, Karsten ; Domratcheva, Tatiana ; Barends, Thomas ; Schlichting, Ilme</creator><creatorcontrib>Gabriela Nass Kovacs ; Jacques-Philippe Colletier ; Grünbein, Marie ; Yang, Yang ; Stensitzki, Till ; Batyuk, Alexander ; Carbajo, Sergio ; Doak, R ; Ehrenberg, David ; Foucar, Lutz ; Gasper, Raphael ; Alexander Gorel ; Hilpert, Mario ; Kloos, Marco ; Koglin, Jason ; Reinstein, Jochen ; Roome, Christopher ; Schlesinger, Ramona ; Seaberg, Matthew ; Shoeman, Robert ; Stricker, Miriam ; Boutet, Sébastien ; Haacke, Stefan ; Heberle, Joachim ; Heyne, Karsten ; Domratcheva, Tatiana ; Barends, Thomas ; Schlichting, Ilme</creatorcontrib><description>Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multi-photon effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.</description><identifier>EISSN: 2331-8422</identifier><identifier>DOI: 10.48550/arxiv.1905.09002</identifier><language>eng</language><publisher>Ithaca: Cornell University Library, arXiv.org</publisher><subject>Amino acids ; Bacteriorhodopsin ; Chromophores ; Crystallography ; Free electron lasers ; Hydrogen bonding ; Organic chemistry ; Photon absorption ; Physics - Biological Physics ; Quantitative Biology - Biomolecules ; Quantum chemistry ; Tryptophan ; Water chemistry</subject><ispartof>arXiv.org, 2019-05</ispartof><rights>2019. This work is published under http://arxiv.org/licenses/nonexclusive-distrib/1.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>http://arxiv.org/licenses/nonexclusive-distrib/1.0</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>228,230,780,784,885,27925</link.rule.ids><backlink>$$Uhttps://doi.org/10.48550/arXiv.1905.09002$$DView paper in arXiv$$Hfree_for_read</backlink><backlink>$$Uhttps://doi.org/10.1038/s41467-019-10758-0$$DView published paper (Access to full text may be restricted)$$Hfree_for_read</backlink></links><search><creatorcontrib>Gabriela Nass Kovacs</creatorcontrib><creatorcontrib>Jacques-Philippe Colletier</creatorcontrib><creatorcontrib>Grünbein, Marie</creatorcontrib><creatorcontrib>Yang, Yang</creatorcontrib><creatorcontrib>Stensitzki, Till</creatorcontrib><creatorcontrib>Batyuk, Alexander</creatorcontrib><creatorcontrib>Carbajo, Sergio</creatorcontrib><creatorcontrib>Doak, R</creatorcontrib><creatorcontrib>Ehrenberg, David</creatorcontrib><creatorcontrib>Foucar, Lutz</creatorcontrib><creatorcontrib>Gasper, Raphael</creatorcontrib><creatorcontrib>Alexander Gorel</creatorcontrib><creatorcontrib>Hilpert, Mario</creatorcontrib><creatorcontrib>Kloos, Marco</creatorcontrib><creatorcontrib>Koglin, Jason</creatorcontrib><creatorcontrib>Reinstein, Jochen</creatorcontrib><creatorcontrib>Roome, Christopher</creatorcontrib><creatorcontrib>Schlesinger, Ramona</creatorcontrib><creatorcontrib>Seaberg, Matthew</creatorcontrib><creatorcontrib>Shoeman, Robert</creatorcontrib><creatorcontrib>Stricker, Miriam</creatorcontrib><creatorcontrib>Boutet, Sébastien</creatorcontrib><creatorcontrib>Haacke, Stefan</creatorcontrib><creatorcontrib>Heberle, Joachim</creatorcontrib><creatorcontrib>Heyne, Karsten</creatorcontrib><creatorcontrib>Domratcheva, Tatiana</creatorcontrib><creatorcontrib>Barends, Thomas</creatorcontrib><creatorcontrib>Schlichting, Ilme</creatorcontrib><title>Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin</title><title>arXiv.org</title><description>Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multi-photon effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.</description><subject>Amino acids</subject><subject>Bacteriorhodopsin</subject><subject>Chromophores</subject><subject>Crystallography</subject><subject>Free electron lasers</subject><subject>Hydrogen bonding</subject><subject>Organic chemistry</subject><subject>Photon absorption</subject><subject>Physics - Biological Physics</subject><subject>Quantitative Biology - Biomolecules</subject><subject>Quantum chemistry</subject><subject>Tryptophan</subject><subject>Water chemistry</subject><issn>2331-8422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GOX</sourceid><recordid>eNotj8tqwzAUREWh0JDmA7qqoGu7eliOtCyhj0BoN94bWb7CCrblSkqa_H3dpKuB4TDMQeiBkryQQpBnHU7umFNFRE4UIewGLRjnNJMFY3doFeOezG25ZkLwBfqsugCQtW6AMTo_6h4fHfxgb_GhT0FbHRNuz6MenInYjXjqfPJwMi5BixttEgTnQ-dbP0U33qNbq_sIq_9courttdp8ZLuv9-3mZZdpwXgmqFS0KKyklgLIpqSSAhFGUW5LaW1DrGG0Ma0GrhiZj9q1asSMt40kpeZL9HidvcjWU3CDDuf6T7q-SM_E05WYgv8-QEz13h_CrBdrxpgqlFSE8191VVsU</recordid><startdate>20190522</startdate><enddate>20190522</enddate><creator>Gabriela Nass Kovacs</creator><creator>Jacques-Philippe Colletier</creator><creator>Grünbein, Marie</creator><creator>Yang, Yang</creator><creator>Stensitzki, Till</creator><creator>Batyuk, Alexander</creator><creator>Carbajo, Sergio</creator><creator>Doak, R</creator><creator>Ehrenberg, David</creator><creator>Foucar, Lutz</creator><creator>Gasper, Raphael</creator><creator>Alexander Gorel</creator><creator>Hilpert, Mario</creator><creator>Kloos, Marco</creator><creator>Koglin, Jason</creator><creator>Reinstein, Jochen</creator><creator>Roome, Christopher</creator><creator>Schlesinger, Ramona</creator><creator>Seaberg, Matthew</creator><creator>Shoeman, Robert</creator><creator>Stricker, Miriam</creator><creator>Boutet, Sébastien</creator><creator>Haacke, Stefan</creator><creator>Heberle, Joachim</creator><creator>Heyne, Karsten</creator><creator>Domratcheva, Tatiana</creator><creator>Barends, Thomas</creator><creator>Schlichting, Ilme</creator><general>Cornell University Library, arXiv.org</general><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>L6V</scope><scope>M7S</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>ALC</scope><scope>GOX</scope></search><sort><creationdate>20190522</creationdate><title>Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin</title><author>Gabriela Nass Kovacs ; Jacques-Philippe Colletier ; Grünbein, Marie ; Yang, Yang ; Stensitzki, Till ; Batyuk, Alexander ; Carbajo, Sergio ; Doak, R ; Ehrenberg, David ; Foucar, Lutz ; Gasper, Raphael ; Alexander Gorel ; Hilpert, Mario ; Kloos, Marco ; Koglin, Jason ; Reinstein, Jochen ; Roome, Christopher ; Schlesinger, Ramona ; Seaberg, Matthew ; Shoeman, Robert ; Stricker, Miriam ; Boutet, Sébastien ; Haacke, Stefan ; Heberle, Joachim ; Heyne, Karsten ; Domratcheva, Tatiana ; Barends, Thomas ; Schlichting, Ilme</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a523-5189144f81f1ee8b6181e05c913f68ffb0fc21bcdae3920553f79b581fdb806a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Amino acids</topic><topic>Bacteriorhodopsin</topic><topic>Chromophores</topic><topic>Crystallography</topic><topic>Free electron lasers</topic><topic>Hydrogen bonding</topic><topic>Organic chemistry</topic><topic>Photon absorption</topic><topic>Physics - Biological Physics</topic><topic>Quantitative Biology - Biomolecules</topic><topic>Quantum chemistry</topic><topic>Tryptophan</topic><topic>Water chemistry</topic><toplevel>online_resources</toplevel><creatorcontrib>Gabriela Nass Kovacs</creatorcontrib><creatorcontrib>Jacques-Philippe Colletier</creatorcontrib><creatorcontrib>Grünbein, Marie</creatorcontrib><creatorcontrib>Yang, Yang</creatorcontrib><creatorcontrib>Stensitzki, Till</creatorcontrib><creatorcontrib>Batyuk, Alexander</creatorcontrib><creatorcontrib>Carbajo, Sergio</creatorcontrib><creatorcontrib>Doak, R</creatorcontrib><creatorcontrib>Ehrenberg, David</creatorcontrib><creatorcontrib>Foucar, Lutz</creatorcontrib><creatorcontrib>Gasper, Raphael</creatorcontrib><creatorcontrib>Alexander Gorel</creatorcontrib><creatorcontrib>Hilpert, Mario</creatorcontrib><creatorcontrib>Kloos, Marco</creatorcontrib><creatorcontrib>Koglin, Jason</creatorcontrib><creatorcontrib>Reinstein, Jochen</creatorcontrib><creatorcontrib>Roome, Christopher</creatorcontrib><creatorcontrib>Schlesinger, Ramona</creatorcontrib><creatorcontrib>Seaberg, Matthew</creatorcontrib><creatorcontrib>Shoeman, Robert</creatorcontrib><creatorcontrib>Stricker, Miriam</creatorcontrib><creatorcontrib>Boutet, Sébastien</creatorcontrib><creatorcontrib>Haacke, Stefan</creatorcontrib><creatorcontrib>Heberle, Joachim</creatorcontrib><creatorcontrib>Heyne, Karsten</creatorcontrib><creatorcontrib>Domratcheva, Tatiana</creatorcontrib><creatorcontrib>Barends, Thomas</creatorcontrib><creatorcontrib>Schlichting, Ilme</creatorcontrib><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Engineering Collection</collection><collection>Engineering Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>arXiv Quantitative Biology</collection><collection>arXiv.org</collection><jtitle>arXiv.org</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gabriela Nass Kovacs</au><au>Jacques-Philippe Colletier</au><au>Grünbein, Marie</au><au>Yang, Yang</au><au>Stensitzki, Till</au><au>Batyuk, Alexander</au><au>Carbajo, Sergio</au><au>Doak, R</au><au>Ehrenberg, David</au><au>Foucar, Lutz</au><au>Gasper, Raphael</au><au>Alexander Gorel</au><au>Hilpert, Mario</au><au>Kloos, Marco</au><au>Koglin, Jason</au><au>Reinstein, Jochen</au><au>Roome, Christopher</au><au>Schlesinger, Ramona</au><au>Seaberg, Matthew</au><au>Shoeman, Robert</au><au>Stricker, Miriam</au><au>Boutet, Sébastien</au><au>Haacke, Stefan</au><au>Heberle, Joachim</au><au>Heyne, Karsten</au><au>Domratcheva, Tatiana</au><au>Barends, Thomas</au><au>Schlichting, Ilme</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin</atitle><jtitle>arXiv.org</jtitle><date>2019-05-22</date><risdate>2019</risdate><eissn>2331-8422</eissn><abstract>Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multi-photon effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.</abstract><cop>Ithaca</cop><pub>Cornell University Library, arXiv.org</pub><doi>10.48550/arxiv.1905.09002</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 2331-8422 |
| ispartof | arXiv.org, 2019-05 |
| issn | 2331-8422 |
| language | eng |
| recordid | cdi_arxiv_primary_1905_09002 |
| source | arXiv.org; Free E- Journals |
| subjects | Amino acids Bacteriorhodopsin Chromophores Crystallography Free electron lasers Hydrogen bonding Organic chemistry Photon absorption Physics - Biological Physics Quantitative Biology - Biomolecules Quantum chemistry Tryptophan Water chemistry |
| title | Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T03%3A44%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_arxiv&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Three-dimensional%20view%20of%20ultrafast%20dynamics%20in%20photoexcited%20bacteriorhodopsin&rft.jtitle=arXiv.org&rft.au=Gabriela%20Nass%20Kovacs&rft.date=2019-05-22&rft.eissn=2331-8422&rft_id=info:doi/10.48550/arxiv.1905.09002&rft_dat=%3Cproquest_arxiv%3E2229498903%3C/proquest_arxiv%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2229498903&rft_id=info:pmid/&rfr_iscdi=true |