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| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| s41598-017-04817-z.pdf | 2.09 MB | Adobe PDF | 見る/開く |
| タイトル: | Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature |
| 著者: | Andersson, Rebecka Safari, Cecilia Dods, Robert Nango, Eriko  Tanaka, Rie  https://orcid.org/0000-0003-1062-4792 (unconfirmed)Yamashita, Ayumi Nakane, Takanori Tono, Kensuke Joti, Yasumasa Båth, Petra Dunevall, Elin Bosman, Robert Nureki, Osamu Iwata, So  Neutze, Richard Brändén, Gisela |
| 著者名の別形: | 南後, 恵理子 岩田, 想 |
| キーワード: | Enzyme mechanisms X-ray crystallography |
| 発行日: | 3-Jul-2017 |
| 出版者: | Springer Nature |
| 誌名: | Scientific Reports |
| 巻: | 7 |
| 論文番号: | 4518 |
| 抄録: | Cytochrome c oxidase catalyses the reduction of molecular oxygen to water while the energy released in this process is used to pump protons across a biological membrane. Although an extremely well-studied biological system, the molecular mechanism of proton pumping by cytochrome c oxidase is still not understood. Here we report a method to produce large quantities of highly diffracting microcrystals of ba3-type cytochrome c oxidase from Thermus thermophilus suitable for serial femtosecond crystallography. The room-temperature structure of cytochrome c oxidase is solved to 2.3 Å resolution from data collected at an X-ray Free Electron Laser. We find overall agreement with earlier X-ray structures solved from diffraction data collected at cryogenic temperature. Previous structures solved from synchrotron radiation data, however, have shown conflicting results regarding the identity of the active-site ligand. Our room-temperature structure, which is free from the effects of radiation damage, reveals that a single-oxygen species in the form of a water molecule or hydroxide ion is bound in the active site. Structural differences between the ba3-type and aa3-type cytochrome c oxidases around the proton-loading site are also described. |
| 著作権等: | © The Author(s) 2017. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. |
| URI: | http://hdl.handle.net/2433/228135 |
| DOI(出版社版): | 10.1038/s41598-017-04817-z |
| PubMed ID: | 28674417 |
| 出現コレクション: | 学術雑誌掲載論文等 |
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