2020年2月
Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
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- 巻
- 1864
- 号
- 2
- 開始ページ
- 129466
- 終了ページ
- 129466
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbagen.2019.129466
- 出版者・発行元
- ELSEVIER
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, damagefree 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.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbagen.2019.129466
- ISSN : 0304-4165
- eISSN : 1872-8006
- PubMed ID : 31678142
- Web of Science ID : WOS:000508740100002