8omx

NI,FE-CODH -600mV state : 1 min Dioxygen Exposure

spinqualitylabelsall models 8omx, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8omx is a 1 chain structure with sequence from Carboxydothermus hydrogenoformans Z-2901. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: FE2, FES, H2S Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COOS2_CARHZ CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) (By similarity). Publication Abstract from PubMed Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of carbon dioxide to carbon monoxide. CODHs are found in anaerobic microorganisms and can rapidly lose their activity when exposed to air. What causes the loss of activity is unclear. In this study, we analyzed the time-dependent structural changes induced by the presence of air on the metal centers of CODH-II. We show that inactivation is a multistep process. In a reversible step, the open coordination site on the Ni ion is blocked by a Ni,Fe-bridging mu-sulfido or chlorido ligand. Blocking this open coordination site with a cyanide ligand stabilizes the cluster against O(2) -induced decomposition, indicating that O(2) attacks at the Ni ion. In the subsequent irreversible phase, nickel is lost, the Fe ions rearrange and the sulfido ligands disappear. Our data are consistent with a reversible reductive reactivation mechanism to protect CODHs from transient over-oxidation. Stepwise O(2) -Induced Rearrangement and Disassembly of the [NiFe(4) (OH)(mu(3) -S)(4) ] Active Site Cluster of CO Dehydrogenase.,Basak Y, Jeoung JH, Domnik L, Dobbek H Angew Chem Int Ed Engl. 2023 Aug 7;62(32):e202305341. doi: , 10.1002/anie.202305341. Epub 2023 Jun 30. PMID:37279092 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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