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

Przemyslaw Nogly; Tobias Weinert; Daniel James; Sergio Carbajo; Dmitry Ozerov; Antonia Furrer; Dardan Gashi; Veniamin Borin; Petr Skopintsev; Kathrin Jaeger; Karol Nass; Petra Båth; Robert Bosman; Jason Koglin; Matthew Seaberg; Thomas Lane; Demet Kekilli; Steffen Brünle; Tomoyuki Tanaka; Wenting Wu; Christopher Milne; Thomas White; Anton Barty; Uwe Weierstall; Valerie Panneels; Eriko Nango; So Iwata; Mark Hunter; Igor Schapiro; Gebhard Schertler; Richard Neutze; Jörg Standfuss

doi:10.1126/science.aat0094

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

Przemyslaw Nogly, Tobias Weinert, Daniel James, Sergio Carbajo, Dmitry Ozerov, Antonia Furrer, Dardan Gashi, Veniamin Borin, Petr Skopintsev, Kathrin Jaeger, Karol Nass, Petra Båth, Robert Bosman, Jason Koglin, Matthew Seaberg, Thomas Lane, Demet Kekilli, Steffen Brünle, Tomoyuki Tanaka, Wenting WuChristopher Milne, Thomas White, Anton Barty, Uwe Weierstall, Valerie Panneels, Eriko Nango, So Iwata, Mark Hunter, Igor Schapiro, Gebhard Schertler, Richard Neutze, Jörg Standfuss

Research output: Contribution to journal › Article › peer-review

237 Scopus citations

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.

Original language	English (US)
Article number	eaat0094
Journal	Science
Volume	361
Issue number	6398
DOIs	https://doi.org/10.1126/science.aat0094
State	Published - Jul 13 2018

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Nogly, P., Weinert, T., James, D., Carbajo, S., Ozerov, D., Furrer, A., Gashi, D., Borin, V., Skopintsev, P., Jaeger, K., Nass, K., Båth, P., Bosman, R., Koglin, J., Seaberg, M., Lane, T., Kekilli, D., Brünle, S., Tanaka, T., ... Standfuss, J. (2018). Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science, 361(6398), Article eaat0094. https://doi.org/10.1126/science.aat0094

Nogly, P, Weinert, T, James, D, Carbajo, S, Ozerov, D, Furrer, A, Gashi, D, Borin, V, Skopintsev, P, Jaeger, K, Nass, K, Båth, P, Bosman, R, Koglin, J, Seaberg, M, Lane, T, Kekilli, D, Brünle, S, Tanaka, T, Wu, W, Milne, C, White, T, Barty, A, Weierstall, U, Panneels, V, Nango, E, Iwata, S, Hunter, M, Schapiro, I, Schertler, G, Neutze, R & Standfuss, J 2018, 'Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser', Science, vol. 361, no. 6398, eaat0094. https://doi.org/10.1126/science.aat0094

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title = "Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser",

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.",

author = "Przemyslaw Nogly and Tobias Weinert and Daniel James and Sergio Carbajo and Dmitry Ozerov and Antonia Furrer and Dardan Gashi and Veniamin Borin and Petr Skopintsev and Kathrin Jaeger and Karol Nass and Petra B{\aa}th and Robert Bosman and Jason Koglin and Matthew Seaberg and Thomas Lane and Demet Kekilli and Steffen Br{\"u}nle and Tomoyuki Tanaka and Wenting Wu and Christopher Milne and Thomas White and Anton Barty and Uwe Weierstall and Valerie Panneels and Eriko Nango and So Iwata and Mark Hunter and Igor Schapiro and Gebhard Schertler and Richard Neutze and J{\"o}rg Standfuss",

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AU - Ozerov, Dmitry

AU - Furrer, Antonia

AU - Gashi, Dardan

AU - Borin, Veniamin

AU - Skopintsev, Petr

AU - Jaeger, Kathrin

AU - Nass, Karol

AU - Båth, Petra

AU - Bosman, Robert

AU - Koglin, Jason

AU - Seaberg, Matthew

AU - Lane, Thomas

AU - Kekilli, Demet

AU - Brünle, Steffen

AU - Tanaka, Tomoyuki

AU - Wu, Wenting

AU - Milne, Christopher

AU - White, Thomas

AU - Barty, Anton

AU - Weierstall, Uwe

AU - Panneels, Valerie

AU - Nango, Eriko

AU - Iwata, So

AU - Hunter, Mark

AU - Schapiro, Igor

AU - Schertler, Gebhard

AU - Neutze, Richard

AU - Standfuss, Jörg

PY - 2018/7/13

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N2 - 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.

AB - 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.

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

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Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 49-406 fs state structure

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: resting state structure

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 457-646 fs state structure

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

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Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 49-406 fs state structure

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: resting state structure

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 457-646 fs state structure

Cite this