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中性子結晶解析の進展が明らかにする酵素反応機構
https://repo.qst.go.jp/records/83163
https://repo.qst.go.jp/records/83163378d76d6-cc2a-4754-bf84-b149c49a60ef
Item type | 一般雑誌記事 / Article(1) | |||||
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公開日 | 2021-02-15 | |||||
タイトル | ||||||
タイトル | 中性子結晶解析の進展が明らかにする酵素反応機構 | |||||
言語 | ||||||
言語 | jpn | |||||
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 | article | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
著者 |
河野, 史明
× 河野, 史明× 栗原, 和男× 玉田, 太郎× Fumiaki, Kono× Kazuo, Kurihara× Taro, Tamada |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Neutron crystallography enables direct observation of hydrogen atoms which play crucial roles in the physiological functions of enzymes, including molecular recognition through hydrogen bonding and catalytic reactions involving proton-coupled electron transfer. Now neutron crystallography is a limited method for protein structure determination, but steadily catholicizes with an operation of diffractometers for bio-macromolecules at neutron facilities and accumulated techniques for sample preparation. In this article, we give a commentary on the current status of neutron crystallography for bio-macromolecules in the world, and illustrate our recent results, neutron structural analyses of copper amine oxidase and copper-containing nitrite reductase, which provide in-depth understandings of the enzymatic reaction mechanism. | |||||
書誌情報 |
生物物理 巻 61, 号 4, p. 216-222, 発行日 2021-07 |
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出版者 | ||||||
出版者 | 日本生物物理学会 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0582-4052 | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.jstage.jst.go.jp/article/biophys/61/4/61_216/_article/-char/ja/ |