5XVC

[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in a ferricyanide-oxidized condition

5XVC の概要

• エントリーDOI: 10.2210/pdb5xvc/pdb
• 分子名称: [NiFe]-hydrogenase 2 large subunit, [NiFe]-hydrogenase 2 small subunit, MAGNESIUM ION, ... (9 entities in total)
• 機能のキーワード: [nife]-hydrogenase, oxidoreductase
• 由来する生物種: Citrobacter sp. S-77; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 196209.64

構造登録者

Nishikawa, K.,Matsuura, H.,Muhd Noor, N.D.,Tai, H.,Hirota, S.,Kim, J.,Kang, J.,Tateno, M.,Yoon, K.S.,Ogo, S.,Shomura, Y.,Higuchi, Y. (登録日: 2017-06-27, 公開日: 2018-06-27, 最終更新日: 2024-10-16)

主引用文献

Noor, N.D.M.,Matsuura, H.,Nishikawa, K.,Tai, H.,Hirota, S.,Kim, J.,Kang, J.,Tateno, M.,Yoon, K.S.,Ogo, S.,Kubota, S.,Shomura, Y.,Higuchi, Y.
Redox-dependent conformational changes of a proximal [4Fe-4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2.
Chem.Commun.(Camb.), 54:12385-12388, 2018

PubMed Abstract: Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe-4S] cluster proximal to the Ni-Fe active site. The presence of relocatable water molecules and a flexible aspartate enables the [4Fe-4S] to display redox-dependent conformational changes. These structural features are proposed to be the key aspects that protect the active site from O2 attack.

PubMed: 30328414
DOI: 10.1039/c8cc06261g

実験手法

X-RAY DIFFRACTION (2.05 Å)