Structural highlights
Publication Abstract from PubMed
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.
Redox-dependent conformational changes of a proximal [4Fe-4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2.,Noor NDM, Matsuura H, Nishikawa K, Tai H, Hirota S, Kim J, Kang J, Tateno M, Yoon KS, Ogo S, Kubota S, Shomura Y, Higuchi Y Chem Commun (Camb). 2018 Oct 30;54(87):12385-12388. doi: 10.1039/c8cc06261g. PMID:30328414[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Noor NDM, Matsuura H, Nishikawa K, Tai H, Hirota S, Kim J, Kang J, Tateno M, Yoon KS, 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). 2018 Oct 30;54(87):12385-12388. doi: 10.1039/c8cc06261g. PMID:30328414 doi:http://dx.doi.org/10.1039/c8cc06261g
