5XVB

[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in an H2-reduced condition

Summary for 5XVB

• Entry DOI: 10.2210/pdb5xvb/pdb
• Descriptor: [NiFe]-hydrogenase 2 large subunit, [NiFe]-hydrogenase 2 small subunit, MAGNESIUM ION, ... (8 entities in total)
• Functional Keywords: [nife]-hydrogenase, oxidoreductase
• Biological source: Citrobacter sp. S-77; More
• Total number of polymer chains: 4
• Total formula weight: 199485.50

Authors

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. (deposition date: 2017-06-27, release date: 2018-06-27, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.84 Å)