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  1. 原著論文

Real-time capture of domain movements during copper amine oxidase catalysis by mix-and-inject serial crystallography

https://repo.qst.go.jp/records/2002701
https://repo.qst.go.jp/records/2002701
0755dbf4-c73a-4447-932d-5a0e066b1676
アイテムタイプ 学術雑誌論文 / Journal Article(1)
公開日 2026-02-09
タイトル
タイトル Real-time capture of domain movements during copper amine oxidase catalysis by mix-and-inject serial crystallography
言語 en
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 Takeshi Murakawa

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Takeshi Murakawa

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Mamoru Suzuki

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Mamoru Suzuki

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Kenji Fukui

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Kenji Fukui

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Tetsuya Masuda

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Tetsuya Masuda

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Eiichi Mizohata

× Eiichi Mizohata

Eiichi Mizohata

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Ikuko Miyahara

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Ikuko Miyahara

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Ikuya Kurauchi

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Ikuya Kurauchi

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Taiki Murakami

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Taiki Murakami

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Himawari Matsunaga

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Himawari Matsunaga

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Yoshiki Montawa

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Yoshiki Montawa

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Norie Nakajima

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Norie Nakajima

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Toshinori Oozeki

× Toshinori Oozeki

Toshinori Oozeki

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Katsuki Sakai

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Katsuki Sakai

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Teikoku Son

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Teikoku Son

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Takehiro Higuchi

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Takehiro Higuchi

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Sunami Tomoko

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Sunami Tomoko

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Tetsunari Kimura

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Tetsunari Kimura

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Kensuke Tono

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Kensuke Tono

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Tomoyuki Tanaka

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Tomoyuki Tanaka

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Michihiro Sugahara

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Michihiro Sugahara

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Toshi Arima

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Toshi Arima

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Luo Fangjia

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Luo Fangjia

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Jungmin Kang

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Jungmin Kang

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Rie Tanaka

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Rie Tanaka

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So Iwata

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So Iwata

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Eriko Nango

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Eriko Nango

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Takehiko Tosha

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Takehiko Tosha

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Takato Yano

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Takato Yano

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Katsuyuki Tanizawa

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Katsuyuki Tanizawa

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Toshihide Okajima

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Toshihide Okajima

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抄録
内容記述タイプ Abstract
内容記述 Protein dynamics play a crucial role in various physiological functions, including enzyme catalysis. To explore conformational changes during enzyme catalysis, we conduct mix-and-inject serial crystallography, an advanced technique to capture time-resolved protein structures in real time, using the microcrystals of bacterial copper amine oxidase containing a protein-derived quinone cofactor. Within 50 ms of mixing the microcrystals (<4 μm) with a preferred substrate (2-phenylethylamine) under anaerobic conditions (reductive half-reaction), we observe domain movements associated with substrate binding and formation of a metastable reaction intermediate, a product Schiff-base of the quinone cofactor. At 100-1000 ms after mixing, conformational transition from aminoresorcinol to the semiquinone radical forms of the reduced cofactor progresses gradually, likely depending on the replacement of the product aldehyde by the next-cycle amine substrate that triggers the cofactor conformational change. Overall, this study provides structural insight into enzyme catalysis accompanying the active-site conformational changes that are hardly scrutinized by studies in solution.
書誌情報 Nature communications

巻 16, 号 1, p. 11149, 発行日 2025-12
出版者
出版者 Springer Nature
PubMed番号
識別子タイプ PMID
関連識別子 41413268
DOI
識別子タイプ DOI
関連識別子 10.1038/s41467-025-67230-5
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