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Structural studies of the NADH-cytochrome b5 reductase

https://repo.qst.go.jp/records/79970
https://repo.qst.go.jp/records/79970
c7661ebf-770d-4253-a2c5-6c8caff4aed0
Item type 会議発表用資料 / Presentation(1)
公開日 2019-12-09
タイトル
タイトル Structural studies of the NADH-cytochrome b5 reductase
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_c94f
資源タイプ conference object
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 Hirano, Yuu

× Hirano, Yuu

WEKO 867970

Hirano, Yuu

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Kurihara, Kazuo

× Kurihara, Kazuo

WEKO 867971

Kurihara, Kazuo

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Kusaka, Katsuhiro

× Kusaka, Katsuhiro

WEKO 867972

Kusaka, Katsuhiro

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Ostermann, Andreas

× Ostermann, Andreas

WEKO 867973

Ostermann, Andreas

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Kimura, Shigenobu

× Kimura, Shigenobu

WEKO 867974

Kimura, Shigenobu

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Miki, Kunio

× Miki, Kunio

WEKO 867975

Miki, Kunio

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Tamada, Taro

× Tamada, Taro

WEKO 867976

Tamada, Taro

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Hirano, Yuu

× Hirano, Yuu

WEKO 867977

en Hirano, Yuu

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Kurihara, Kazuo

× Kurihara, Kazuo

WEKO 867978

en Kurihara, Kazuo

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Tamada, Taro

× Tamada, Taro

WEKO 867979

en Tamada, Taro

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抄録
内容記述タイプ Abstract
内容記述 Information about hydrogen atoms and valence electrons is important to understand functions of electron transfer proteins, because they are directly connected with the reactivity of redox reactions. In the redox proteins, the possibility of quantum tunneling has been discussed on the hydrogen and electron transfer reactions. Therefore, high-resolution structural information is required to detect small structural changes due to the redox reactions. The NADH-cytochrome b5 reductase (b5R) and cytochrome b5 (b5) redox system is involved in various electron transfer reactions, such as lipid unsaturation, cholesterol synthesis and drug metabolism. The X-ray crystal structure of oxidized form of b5R at 0.78 Å resolution clearly visualized valence electron densities of the FAD cofactor. The X-ray crystal structures of the oxidized and reduced forms of b5 shows small structural changes between two redox states. We have recently determined the neutron crystal structures of the oxidized form of b5R at 1.4 Å resolution. In addition, we have determined high-resolution X-ray crystal structures of the reduced form of b5R. The neutron and X-ray structure analyses provide information about the hydrogen transfer pathway in b5R.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 3rd QST International Symposium
発表年月日
日付 2019-12-04
日付タイプ Issued
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