ID | 57859 |
フルテキストURL | |
著者 |
Suga, Michihiro
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Shimada, Atsuhiro
Graduate School of Applied Biological Sciences and Faculty of Applied Biological Sciences, Gifu University
Akita, Fusamichi
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Shen, Jian-Ren
Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
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Tosha, Takehiko
Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center
Sugimoto, Hiroshi
Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center
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抄録 | Background: The invention of the X-ray free-electron laser (XFEL) has provided unprecedented new opportunities for structural biology. The advantage of XFEL is an intense pulse of X-rays and a very short pulse duration (<10 fs) promising a damage-free and time-resolved crystallography approach.
Scope of review: Recent time-resolved crystallographic analyses in XFEL facility SACLA are reviewed. Specifically, metalloproteins involved in the essential reactions of bioenergy conversion including photosystem II, cytochrome c oxidase and nitric oxide reductase are described. Major conclusions: XFEL with pump-probe techniques successfully visualized the process of the reaction and the dynamics of a protein. Since the active center of metalloproteins is very sensitive to the X-ray radiation, damage-free structures obtained by XFEL are essential to draw mechanistic conclusions. Methods and tools for sample delivery and reaction initiation are key for successful measurement of the time-resolved data. General significance: XFEL is at the center of approaches to gain insight into complex mechanism of structural dynamics and the reactions catalyzed by biological macromolecules. Further development has been carried out to expand the application of time-resolved X-ray crystallography. This article is part of a Special Issue entitled Novel measurement techniques for visualizing 'live' protein molecules. |
キーワード | Heme
Metalloproteins
Proton pump
Radiation damage
Serial femtosecond crystallography
X-ray free-electron laser
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発行日 | 2020-02-29
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出版物タイトル |
Biochimica et Biophysica Acta (BBA) - General Subjects
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巻 | 1864巻
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号 | 2号
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出版者 | SI
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開始ページ | 129466
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ISSN | 03044165
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NCID | AA00564679
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資料タイプ |
学術雑誌論文
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言語 |
英語
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OAI-PMH Set |
岡山大学
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著作権者 | © 2019 The Author(s). Published by Elsevier B.V.
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論文のバージョン | publisher
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PubMed ID | |
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関連URL | isVersionOf https://doi.org/10.1016/j.bbagen.2019.129466
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ライセンス | http://creativecommons.org/licenses/by/4.0/
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Citation | Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto, Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA, Biochimica et Biophysica Acta (BBA) - General Subjects, Volume 1864, Issue 2, 2020, 129466, ISSN 0304-4165, https://doi.org/10.1016/j.bbagen.2019.129466.
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助成機関名 |
日本学術振興会
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助成番号 | 15H01642
17H05884
15H01655
17H05896
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オープンアクセス(出版社) |
OA
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オープンアーカイブ(出版社) |
非OpenArchive
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