8pou

Crystal Structure of the C19G/C120G variant of the membrane-bound [NiFe]-Hydrogenase from Cupriavidus necator in the air-oxidized state at 1.65 A Resolution.

spinqualitylabelsall models 8pou, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8pou is a 2 chain structure with sequence from Cupriavidus necator H16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: CL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MBHL_CUPNH This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. Publication Abstract from PubMed The membrane-bound [NiFe]-hydrogenase of Cupriavidus necator is a rare example of a truly O(2)-tolerant hydrogenase. It catalyzes the oxidation of H(2) into 2e(-) and 2H(+) in the presence of high O(2) concentrations. This characteristic trait is intimately linked to the unique Cys(6)[4Fe-3S] cluster located in the proximal position to the catalytic center and coordinated by six cysteine residues. Two of these cysteines play an essential role in redox-dependent cluster plasticity, which bestows the cofactor with the capacity to mediate two redox transitions at physiological potentials. Here, we investigated the individual roles of the two additional cysteines by replacing them individually as well as simultaneously with glycine. The crystal structures of the corresponding MBH variants revealed the presence of Cys(5)[4Fe-4S] or Cys(4)[4Fe-4S] clusters of different architecture. The protein X-ray crystallography results were correlated with accompanying biochemical, spectroscopic and electrochemical data. The exchanges resulted in a diminished O(2) tolerance of all MBH variants, which was attributed to the fact that the modified proximal clusters mediated only one redox transition. The previously proposed O(2) protection mechanism that detoxifies O(2) to H(2)O using four protons and four electrons supplied by the cofactor infrastructure, is extended by our results, which suggest efficient shutdown of enzyme function by formation of a hydroxy ligand in the active site that protects the enzyme from O(2) binding under electron-deficient conditions. Stepwise conversion of the Cys(6)[4Fe-3S] to a Cys(4)[4Fe-4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase.,Schmidt A, Kalms J, Lorent C, Katz S, Frielingsdorf S, Evans RM, Fritsch J, Siebert E, Teutloff C, Armstrong FA, Zebger I, Lenz O, Scheerer P Chem Sci. 2023 Sep 20;14(40):11105-11120. doi: 10.1039/d3sc03739h. eCollection , 2023 Oct 18. PMID:37860641 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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