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New insights into the catalytic active-site structure of multicopper oxidases
http://hdl.handle.net/2297/38226
http://hdl.handle.net/2297/38226656703c7-e49d-40af-897b-32e99cfc8016
名前 / ファイル | ライセンス | アクション |
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SC-PR-SAKURAI-T-772.pdf (1.1 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2017-10-03 | |||||
タイトル | ||||||
タイトル | New insights into the catalytic active-site structure of multicopper oxidases | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Komori, Hirofumi
× Komori, Hirofumi× Sugiyama, Ryosuke× Kataoka, Kunishige× Miyazaki, Kentaro× Higuchi, Yoshiki× Sakurai, Takeshi |
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書誌情報 |
Acta Crystallographica Section D: Biological Crystallography 巻 70, 号 3, p. 772-779, 発行日 2014-03-01 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1399-0047 | |||||
NCID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA12097672 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1107/S1399004713033051 | |||||
出版者 | ||||||
出版者 | International Union of Crystallography | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Structural models determined by X-ray crystallography play a central role in understanding the catalytic mechanism of enzymes. However, X-ray radiation generates hydrated electrons that can cause significant damage to the active sites of metalloenzymes. In the present study, crystal structures of the multicopper oxidases (MCOs) CueO from Escherichia coli and laccase from a metagenome were determined. Diffraction data were obtained from a single crystal under low to high X-ray dose conditions. At low levels of X-ray exposure, unambiguous electron density for an O atom was observed inside the trinuclear copper centre (TNC) in both MCOs. The gradual reduction of copper by hydrated electrons monitored by measurement of the Cu K-edge X-ray absorption spectra led to the disappearance of the electron density for the O atom. In addition, the size of the copper triangle was enlarged by a two-step shift in the location of the type III coppers owing to reduction. Further, binding of O2 to the TNC after its full reduction was observed in the case of the laccase. Based on these novel structural findings, the diverse resting structures of the MCOs and their four-electron O2-reduction process are discussed. © 2014 International Union of Crystallography. | |||||
権利 | ||||||
権利情報 | Copyright © International Union of Crystallography | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
関連URI | ||||||
識別子タイプ | URI | |||||
関連識別子 | http://scripts.iucr.org/cgi-bin/paper?S1399004713033051 |