Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser

Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion transport across bacterial membranes. We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacte...

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Published in:Science (American Association for the Advancement of Science) 2018-07, Vol.361 (6398)
Main Authors: Nogly, Przemyslaw, Weinert, Tobias, James, Daniel, Carbajo, Sergio, Ozerov, Dmitry, Furrer, Antonia, Gashi, Dardan, Borin, Veniamin, Skopintsev, Petr, Jaeger, Kathrin, Nass, Karol, Båth, Petra, Bosman, Robert, Koglin, Jason, Seaberg, Matthew, Lane, Thomas, Kekilli, Demet, Brünle, Steffen, Tanaka, Tomoyuki, Wu, Wenting, Milne, Christopher, White, Thomas, Barty, Anton, Weierstall, Uwe, Panneels, Valerie, Nango, Eriko, Iwata, So, Hunter, Mark, Schapiro, Igor, Schertler, Gebhard, Neutze, Richard, Standfuss, Jörg
Format: Article
Language:English
Subjects:
Analytical Chemistry
Analytisk kemi
Aspartic acid
Aspartic Acid - chemistry
Atomic properties
Atomic structure
Bacteriorhodopsin
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - radiation effects
BASIC BIOLOGICAL SCIENCES
Biological activity
Charge distribution
Charge transfer
Chemical reactions
Chromophores
Circadian rhythms
Coherent light
Crystal structure
Crystallography
Dynamic structural analysis
Electrochemistry
Evolution
excited-state dynamics
free-electron lasers
Imines
Information processing
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Integral membrane proteins
Intermediates
Ion Transport
Isomerism
Isomerization
Lasers
Light
Light sources
Mechanics (Physics)
Membranes
Microcrystals
Molecular chains
photoactive yellow protein
Photochemical reactions
Photochemicals
photoisomerization
primary photochemical event
Protein Conformation
Proteins
Protons
Proximity
Quantum mechanics
Radiation
Residues
resolved serial crystallography
Retina
Retinal-binding protein
Retinaldehyde - chemistry
Retinaldehyde - radiation effects
Schiff Bases - chemistry
schiff-base
Science & Technology - Other Topics
source
Spatial resolution
spectroscopy
Stereoselectivity
structural-changes
Time Factors
Timing
Water
Water - chemistry
X-ray diffraction
X-Rays
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cited_by cdi_FETCH-LOGICAL-c431t-d7b9f0053f109b065effba61eb954ab4d1d62c7a7ebef12dd3da1f8b398e5e843
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container_issue 6398
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container_title Science (American Association for the Advancement of Science)
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creator Nogly, Przemyslaw
Weinert, Tobias
James, Daniel
Carbajo, Sergio
Ozerov, Dmitry
Furrer, Antonia
Gashi, Dardan
Borin, Veniamin
Skopintsev, Petr
Jaeger, Kathrin
Nass, Karol
Båth, Petra
Bosman, Robert
Koglin, Jason
Seaberg, Matthew
Lane, Thomas
Kekilli, Demet
Brünle, Steffen
Tanaka, Tomoyuki
Wu, Wenting
Milne, Christopher
White, Thomas
Barty, Anton
Weierstall, Uwe
Panneels, Valerie
Nango, Eriko
Iwata, So
Hunter, Mark
Schapiro, Igor
Schertler, Gebhard
Neutze, Richard
Standfuss, Jörg
description Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion transport across bacterial membranes. We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key facet of this stereoselective and efficient photochemical reaction.
doi_str_mv 10.1126/science.aat0094
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We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key facet of this stereoselective and efficient photochemical reaction.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aat0094</identifier><identifier>PMID: 29903883</identifier><language>eng</language><publisher>United States: The American Association for the Advancement of Science</publisher><subject>Analytical Chemistry ; Analytisk kemi ; Aspartic acid ; Aspartic Acid - chemistry ; Atomic properties ; Atomic structure ; Bacteriorhodopsin ; Bacteriorhodopsins - chemistry ; Bacteriorhodopsins - radiation effects ; BASIC BIOLOGICAL SCIENCES ; Biological activity ; Charge distribution ; Charge transfer ; Chemical reactions ; Chromophores ; Circadian rhythms ; Coherent light ; Crystal structure ; Crystallography ; Dynamic structural analysis ; Electrochemistry ; Evolution ; excited-state dynamics ; free-electron lasers ; Imines ; Information processing ; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY ; Integral membrane proteins ; Intermediates ; Ion Transport ; Isomerism ; Isomerization ; Lasers ; Light ; Light sources ; Mechanics (Physics) ; Membranes ; Microcrystals ; Molecular chains ; photoactive yellow protein ; Photochemical reactions ; Photochemicals ; photoisomerization ; primary photochemical event ; Protein Conformation ; Proteins ; Protons ; Proximity ; Quantum mechanics ; Radiation ; Residues ; resolved serial crystallography ; Retina ; Retinal-binding protein ; Retinaldehyde - chemistry ; Retinaldehyde - radiation effects ; Schiff Bases - chemistry ; schiff-base ; Science &amp; Technology - Other Topics ; source ; Spatial resolution ; spectroscopy ; Stereoselectivity ; structural-changes ; Time Factors ; Timing ; Water ; Water - chemistry ; X-ray diffraction ; X-Rays</subject><ispartof>Science (American Association for the Advancement of Science), 2018-07, Vol.361 (6398)</ispartof><rights>Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. 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We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. 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isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser</title><author>Nogly, Przemyslaw ; Weinert, Tobias ; James, Daniel ; Carbajo, Sergio ; Ozerov, Dmitry ; Furrer, Antonia ; Gashi, Dardan ; Borin, Veniamin ; Skopintsev, Petr ; Jaeger, Kathrin ; Nass, Karol ; Båth, Petra ; Bosman, Robert ; Koglin, Jason ; Seaberg, Matthew ; Lane, Thomas ; Kekilli, Demet ; Brünle, Steffen ; Tanaka, Tomoyuki ; Wu, Wenting ; Milne, Christopher ; White, Thomas ; Barty, Anton ; Weierstall, Uwe ; Panneels, Valerie ; Nango, Eriko ; Iwata, So ; Hunter, Mark ; Schapiro, Igor ; Schertler, Gebhard ; Neutze, Richard ; Standfuss, Jörg</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-d7b9f0053f109b065effba61eb954ab4d1d62c7a7ebef12dd3da1f8b398e5e843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Analytical Chemistry</topic><topic>Analytisk kemi</topic><topic>Aspartic acid</topic><topic>Aspartic Acid - chemistry</topic><topic>Atomic properties</topic><topic>Atomic structure</topic><topic>Bacteriorhodopsin</topic><topic>Bacteriorhodopsins - chemistry</topic><topic>Bacteriorhodopsins - radiation effects</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Biological activity</topic><topic>Charge distribution</topic><topic>Charge transfer</topic><topic>Chemical reactions</topic><topic>Chromophores</topic><topic>Circadian rhythms</topic><topic>Coherent light</topic><topic>Crystal structure</topic><topic>Crystallography</topic><topic>Dynamic structural analysis</topic><topic>Electrochemistry</topic><topic>Evolution</topic><topic>excited-state dynamics</topic><topic>free-electron lasers</topic><topic>Imines</topic><topic>Information processing</topic><topic>INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY</topic><topic>Integral membrane proteins</topic><topic>Intermediates</topic><topic>Ion Transport</topic><topic>Isomerism</topic><topic>Isomerization</topic><topic>Lasers</topic><topic>Light</topic><topic>Light sources</topic><topic>Mechanics (Physics)</topic><topic>Membranes</topic><topic>Microcrystals</topic><topic>Molecular chains</topic><topic>photoactive yellow protein</topic><topic>Photochemical reactions</topic><topic>Photochemicals</topic><topic>photoisomerization</topic><topic>primary photochemical event</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Protons</topic><topic>Proximity</topic><topic>Quantum mechanics</topic><topic>Radiation</topic><topic>Residues</topic><topic>resolved serial crystallography</topic><topic>Retina</topic><topic>Retinal-binding protein</topic><topic>Retinaldehyde - chemistry</topic><topic>Retinaldehyde - radiation effects</topic><topic>Schiff Bases - chemistry</topic><topic>schiff-base</topic><topic>Science &amp; Technology - Other Topics</topic><topic>source</topic><topic>Spatial resolution</topic><topic>spectroscopy</topic><topic>Stereoselectivity</topic><topic>structural-changes</topic><topic>Time Factors</topic><topic>Timing</topic><topic>Water</topic><topic>Water - chemistry</topic><topic>X-ray diffraction</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nogly, Przemyslaw</creatorcontrib><creatorcontrib>Weinert, Tobias</creatorcontrib><creatorcontrib>James, Daniel</creatorcontrib><creatorcontrib>Carbajo, Sergio</creatorcontrib><creatorcontrib>Ozerov, Dmitry</creatorcontrib><creatorcontrib>Furrer, Antonia</creatorcontrib><creatorcontrib>Gashi, Dardan</creatorcontrib><creatorcontrib>Borin, Veniamin</creatorcontrib><creatorcontrib>Skopintsev, Petr</creatorcontrib><creatorcontrib>Jaeger, Kathrin</creatorcontrib><creatorcontrib>Nass, Karol</creatorcontrib><creatorcontrib>Båth, Petra</creatorcontrib><creatorcontrib>Bosman, Robert</creatorcontrib><creatorcontrib>Koglin, Jason</creatorcontrib><creatorcontrib>Seaberg, Matthew</creatorcontrib><creatorcontrib>Lane, Thomas</creatorcontrib><creatorcontrib>Kekilli, Demet</creatorcontrib><creatorcontrib>Brünle, Steffen</creatorcontrib><creatorcontrib>Tanaka, Tomoyuki</creatorcontrib><creatorcontrib>Wu, Wenting</creatorcontrib><creatorcontrib>Milne, Christopher</creatorcontrib><creatorcontrib>White, Thomas</creatorcontrib><creatorcontrib>Barty, Anton</creatorcontrib><creatorcontrib>Weierstall, Uwe</creatorcontrib><creatorcontrib>Panneels, Valerie</creatorcontrib><creatorcontrib>Nango, Eriko</creatorcontrib><creatorcontrib>Iwata, So</creatorcontrib><creatorcontrib>Hunter, Mark</creatorcontrib><creatorcontrib>Schapiro, Igor</creatorcontrib><creatorcontrib>Schertler, Gebhard</creatorcontrib><creatorcontrib>Neutze, Richard</creatorcontrib><creatorcontrib>Standfuss, Jörg</creatorcontrib><creatorcontrib>SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United 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Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nogly, Przemyslaw</au><au>Weinert, Tobias</au><au>James, Daniel</au><au>Carbajo, Sergio</au><au>Ozerov, Dmitry</au><au>Furrer, Antonia</au><au>Gashi, Dardan</au><au>Borin, Veniamin</au><au>Skopintsev, Petr</au><au>Jaeger, Kathrin</au><au>Nass, Karol</au><au>Båth, Petra</au><au>Bosman, Robert</au><au>Koglin, Jason</au><au>Seaberg, Matthew</au><au>Lane, Thomas</au><au>Kekilli, Demet</au><au>Brünle, Steffen</au><au>Tanaka, Tomoyuki</au><au>Wu, Wenting</au><au>Milne, Christopher</au><au>White, Thomas</au><au>Barty, Anton</au><au>Weierstall, Uwe</au><au>Panneels, Valerie</au><au>Nango, Eriko</au><au>Iwata, So</au><au>Hunter, Mark</au><au>Schapiro, Igor</au><au>Schertler, Gebhard</au><au>Neutze, Richard</au><au>Standfuss, Jörg</au><aucorp>SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2018-07-13</date><risdate>2018</risdate><volume>361</volume><issue>6398</issue><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion transport across bacterial membranes. We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key facet of this stereoselective and efficient photochemical reaction.</abstract><cop>United States</cop><pub>The American Association for the Advancement of Science</pub><pmid>29903883</pmid><doi>10.1126/science.aat0094</doi><orcidid>https://orcid.org/0000-0001-8825-386X</orcidid><orcidid>https://orcid.org/0000-0002-8040-7753</orcidid><orcidid>https://orcid.org/0000-0001-6811-6083</orcidid><orcidid>https://orcid.org/0000-0003-1735-2937</orcidid><orcidid>https://orcid.org/0000-0003-4714-9139</orcidid><orcidid>https://orcid.org/0000-0001-9894-6985</orcidid><orcidid>https://orcid.org/0000-0002-8407-0270</orcidid><orcidid>https://orcid.org/0000-0001-8843-1566</orcidid><orcidid>https://orcid.org/0000-0002-3594-930X</orcidid><orcidid>https://orcid.org/0000-0002-0339-3722</orcidid><orcidid>https://orcid.org/0000-0003-2627-4432</orcidid><orcidid>https://orcid.org/0000-0001-7832-1443</orcidid><orcidid>https://orcid.org/0000-0002-5292-4470</orcidid><orcidid>https://orcid.org/0000-0003-0986-6153</orcidid><orcidid>https://orcid.org/0000-0001-8536-6869</orcidid><orcidid>https://orcid.org/0000-0002-5846-6810</orcidid><orcidid>https://orcid.org/0000-0002-4560-4698</orcidid><orcidid>https://orcid.org/0000-0001-9851-7355</orcidid><orcidid>https://orcid.org/0000-0002-8348-6661</orcidid><orcidid>https://orcid.org/000000018825386X</orcidid><orcidid>https://orcid.org/0000000309866153</orcidid><orcidid>https://orcid.org/0000000280407753</orcidid><orcidid>https://orcid.org/0000000198946985</orcidid><orcidid>https://orcid.org/000000023594930X</orcidid><orcidid>https://orcid.org/0000000178321443</orcidid><orcidid>https://orcid.org/0000000168116083</orcidid><orcidid>https://orcid.org/0000000203393722</orcidid><orcidid>https://orcid.org/0000000252924470</orcidid><orcidid>https://orcid.org/0000000245604698</orcidid><orcidid>https://orcid.org/0000000185366869</orcidid><orcidid>https://orcid.org/0000000258466810</orcidid><orcidid>https://orcid.org/0000000283486661</orcidid><orcidid>https://orcid.org/0000000284070270</orcidid><orcidid>https://orcid.org/0000000188431566</orcidid><orcidid>https://orcid.org/0000000326274432</orcidid><orcidid>https://orcid.org/0000000317352937</orcidid><orcidid>https://orcid.org/0000000347149139</orcidid><orcidid>https://orcid.org/0000000198517355</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0036-8075
ispartof Science (American Association for the Advancement of Science), 2018-07, Vol.361 (6398)
issn 0036-8075
1095-9203
language eng
recordid cdi_swepub_primary_oai_gup_ub_gu_se_269505
source Alma/SFX Local Collection; JSTOR; Science
subjects Analytical Chemistry
Analytisk kemi
Aspartic acid
Aspartic Acid - chemistry
Atomic properties
Atomic structure
Bacteriorhodopsin
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - radiation effects
BASIC BIOLOGICAL SCIENCES
Biological activity
Charge distribution
Charge transfer
Chemical reactions
Chromophores
Circadian rhythms
Coherent light
Crystal structure
Crystallography
Dynamic structural analysis
Electrochemistry
Evolution
excited-state dynamics
free-electron lasers
Imines
Information processing
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Integral membrane proteins
Intermediates
Ion Transport
Isomerism
Isomerization
Lasers
Light
Light sources
Mechanics (Physics)
Membranes
Microcrystals
Molecular chains
photoactive yellow protein
Photochemical reactions
Photochemicals
photoisomerization
primary photochemical event
Protein Conformation
Proteins
Protons
Proximity
Quantum mechanics
Radiation
Residues
resolved serial crystallography
Retina
Retinal-binding protein
Retinaldehyde - chemistry
Retinaldehyde - radiation effects
Schiff Bases - chemistry
schiff-base
Science & Technology - Other Topics
source
Spatial resolution
spectroscopy
Stereoselectivity
structural-changes
Time Factors
Timing
Water
Water - chemistry
X-ray diffraction
X-Rays
title Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser
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