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Catalytic mechanism of the tyrosinase reaction toward the Tyr98 residue in the caddie protein

https://hiroshima.repo.nii.ac.jp/records/2007927
https://hiroshima.repo.nii.ac.jp/records/2007927
9e4e4015-d9c7-420c-84b1-24482e85aa9c
名前 / ファイル ライセンス アクション
PLoSBiol_16_e300007.pdf PLoSBiol_16_e300007.pdf (2.4 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Catalytic mechanism of the tyrosinase reaction toward the Tyr98 residue in the caddie protein
言語 en
作成者 Matoba, Yasuyuki

× Matoba, Yasuyuki

en Matoba, Yasuyuki

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Kihara, Shogo

× Kihara, Shogo

en Kihara, Shogo

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Bando, Naohiko

× Bando, Naohiko

en Bando, Naohiko

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Yoshitsu, Hironari

× Yoshitsu, Hironari

en Yoshitsu, Hironari

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Sakaguchi, Miyuki

× Sakaguchi, Miyuki

en Sakaguchi, Miyuki

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Kayama, Kure'e

× Kayama, Kure'e

en Kayama, Kure'e

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Yanagisawa, Sachiko

× Yanagisawa, Sachiko

en Yanagisawa, Sachiko

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Ogura, Takashi

× Ogura, Takashi

en Ogura, Takashi

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Sugiyama, Masanori

× Sugiyama, Masanori

en Sugiyama, Masanori

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 © 2018 Matoba et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
内容記述
内容記述 Tyrosinase (EC 1.14.18.1), a copper-containing monooxygenase, catalyzes the conversion of phenol to the corresponding ortho-quinone. The Streptomyces tyrosinase is generated as a complex with a “caddie" protein that facilitates the transport of two copper ions into the active center. In our previous study, the Tyr98 residue in the caddie protein, which is accommodated in the pocket of active center of tyrosinase, has been found to be converted to a reactive quinone through the formations of the μ-η2:η2-peroxo-dicopper(II) and Cu(II)-dopasemiquinone intermediates. Until now—despite extensive studies for the tyrosinase reaction based on the crystallographic analysis, low-molecular-weight models, and computer simulations—the catalytic mechanism has been unable to be made clear at an atomic level. To make the catalytic mechanism of tyrosinase clear, in the present study, the cryo-trapped crystal structures were determined at very high resolutions (1.16–1.70 Å). The structures suggest the existence of an important step for the tyrosinase reaction that has not yet been found: that is, the hydroxylation reaction is triggered by the movement of CuA, which induces the syn-to-anti rearrangement of the copper ligands after the formation of μ-η2:η2-peroxo-dicopper(II) core. By the rearrangement, the hydroxyl group of the substrate is placed in an equatorial position, allowing the electrophilic attack to the aromatic ring by the Cu2O2 oxidant.
言語 en
内容記述
内容記述タイプ Other
内容記述 This study was partly supported by grants (nos. 25109530 and 15H009470 to YM, and 25109540 and 15H00960 to TO, Stimuli-Responsive Chemical Species) for Scientific Research on Innovative Areas and by a grant for Scientific Research (22550153 to MS) from MEXT of Japan. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
出版者
出版者 Public Library of Science
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
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1371/journal.pbio.3000077
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1371/journal.pbio.3000077
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1544-9173
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1545-7885
開始ページ
開始ページ e3000077
書誌情報 PLoS Biology
PLoS Biology

巻 16, 号 12, p. e3000077, 発行日 2018-12-31
旧ID 48619
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