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  Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

Pande, K., Hutchison, C. D. M., Groenhof, G., Aquila, A., Robinson, J. S., Tenboer, J., Basu, S., Boutet, S., DePonte, D. P., Liang, M., White, T. A., Zatsepin, N. A., Yefanov, O., Morozov, D., Oberthuer, D., Gati, C., Subramanian, G., James, D., Zhao, Y., Koralek, J., Brayshaw, J., Kupitz, C., Conrad, C., Roy-Chowdhury, S., Coe, J. D., Metz, M., Paulraj, L. X., Grant, T. D., Koglin, J. E., Ketawala, G., Fromme, R., Šrajer, V., Henning, R., Spence, J. C. H., Ourmazd, A., Schwander, P., Weierstall, U., Frank, M., Fromme, P., Barty, A., Chapman, H. N., Moffat, K., van Thor, J. J., & Schmidt, M. (2016). Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein. Science, 352(6286), 725-729. doi:10.1126/science.aad5081.

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アイテムのパーマリンク: https://hdl.handle.net/11858/00-001M-0000-002A-D6E4-C 版のパーマリンク: https://hdl.handle.net/21.11116/0000-0007-0EC1-0
資料種別: 学術論文

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URL:
http://dx.doi.org/10.1126/science.aad5081 (出版社版)
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作成者

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 作成者:
Pande, Kanupriya1, 2, 著者
Hutchison, Christopher D. M.3, 著者
Groenhof, Gerrit4, 著者
Aquila, Andy5, 著者
Robinson, Josef S.5, 著者
Tenboer, Jason1, 著者
Basu, Shibom6, 著者
Boutet, Sébastien5, 著者
DePonte, Daniel P.5, 著者
Liang, Mengning5, 著者
White, Thomas A.2, 著者
Zatsepin, Nadia A.7, 著者
Yefanov, Oleksandr2, 著者
Morozov, Dmitry4, 著者
Oberthuer, Dominik2, 著者
Gati, Cornelius2, 著者
Subramanian, Ganesh7, 著者
James, Daniel7, 著者
Zhao, Yun7, 著者
Koralek, Jake5, 著者
Brayshaw, Jennifer1, 著者Kupitz, Christopher1, 著者Conrad, Chelsie6, 著者Roy-Chowdhury, Shatabdi6, 著者Coe, Jesse D.6, 著者Metz, Markus2, 著者Paulraj, Lourdu Xavier2, 8, 著者           Grant, Thomas D.9, 著者Koglin, Jason E.5, 著者Ketawala, Gihan6, 著者Fromme, Raimund6, 著者Šrajer, Vukica10, 著者Henning, Robert10, 著者Spence, John C. H.7, 著者Ourmazd, Abbas1, 著者Schwander, Peter1, 著者Weierstall, Uwe7, 著者Frank, Matthias11, 著者Fromme, Petra6, 著者Barty, Anton2, 著者Chapman, Henry N.2, 12, 著者Moffat, Keith10, 13, 著者van Thor, Jasper J.3, 著者Schmidt, Marius1, 著者 全て表示
所属:
1Department of Physics, University of Wisconsin–Milwaukee, Milwaukee, WI 53211, USA, ou_persistent22              
2Center for Free Electron Laser Science, Deutsches Elektronen Synchrotron, Notkestrasse 85, 22607 Hamburg, Germany, ou_persistent22              
3Faculty of Natural Sciences, Department of Life Sciences, Imperial College, London SW7 2AZ, UK, ou_persistent22              
4Nanoscience Center and Department of Chemistry, University of Jyväskylä, Post Office Box 35, 40014 Jyväskylä, Finland, ou_persistent22              
5Linac Coherent Light Source, SLAC National Accelerator Laboratory, Sand Hill Road, Menlo Park, CA 94025, USA, ou_persistent22              
6School of Molecular Sciences and Biodesign Center for Applied Structural Discovery, Arizona State University, Tempe, AZ 85287, USA, ou_persistent22              
7Department of Physics, Arizona State University, Tempe, AZ 85287, USA, ou_persistent22              
8International Max Planck Research School for Ultrafast Imaging & Structural Dynamics (IMPRS-UFAST), Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2266714              
9Hauptman-Woodward Institute, State University of New York at Buffalo, 700 Ellicott Street, Buffalo, NY 14203, USA, ou_persistent22              
10Center for Advanced Radiation Sources, University of Chicago, Chicago, IL 60637, USA, ou_persistent22              
11Lawrence Livermore National Laboratory, Livermore, CA 94550, USA, ou_persistent22              
12Center for Ultrafast Imaging, University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany, ou_persistent22              
13Department of Biochemistry and Molecular Biology and Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA, ou_persistent22              

内容説明

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キーワード: -
 要旨: A variety of organisms have evolved mechanisms to detect and respond to light, in which the response is mediated by protein structural changes after photon absorption. The initial step is often the photoisomerization of a conjugated chromophore. Isomerization occurs on ultrafast time scales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans-to-cis isomerization of the chromophore in photoactive yellow protein. Femtosecond hard x-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on photoactive yellow protein microcrystals over a time range from 100 femtoseconds to 3 picoseconds to determine the structural dynamics of the photoisomerization reaction.

資料詳細

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言語: eng - English
 日付: 2015-09-272016-04-052016-05-062016-05-06
 出版の状態: 出版
 ページ: 5
 出版情報: -
 目次: -
 査読: 査読あり
 識別子（DOI, ISBNなど）: DOI: 10.1126/science.aad5081
 学位: -

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出版物 1

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出版物名: Science
種別: 学術雑誌
 著者・編者:
所属:
出版社, 出版地: Washington, D.C. : American Association for the Advancement of Science
ページ: - 巻号: 352 (6286) 通巻号: - 開始・終了ページ: 725 - 729 識別子（ISBN, ISSN, DOIなど）: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1