5y4n

Crystal structure of aerobically purified and anaerobically crystallized D. vulgaris Miyazaki F [NiFe]-hydrogenase

spinqualitylabelsall models 5y4n, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y4n is a 2 chain structure with sequence from Desulfovibrio vulgaris str. 'Miyazaki F'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: CSO, MG, MPD, MRD, NFU, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHNS_NITV9 Catalyzes the reversible oxidoreduction of molecular hydrogen, in conjunction with a specific electron acceptor, cytochrome c3. Publication Abstract from PubMed Hydrogenase is a key enzyme for a coming hydrogen energy society, because it has strong catalytic activities on both uptake and production of dihydrogen. We, however, have to overcome the sensitivity against O2 of the enzyme, because hydrogenase is, generally, easily inactivated in the presence of O2. In this study, we have revisited the crystal structures of [NiFe]hydrogenase from sulfate-reducing bacterium in the several oxidized and reduced conditions. Our results revealed that the Ni-Fe active site of the enzyme exposed into O2 showed two forms, Form-1 and Form-2. The Ni-Fe active site in Form-1 showed the typical Ni-B (inactive ready) structure, whereas those in Form-2 lost Ni with no relation to an exposure time to O2, and two cysteinyl sulfur ligands made a disulfide bond. On the other hand, the formation of sulfenylation of the cysteinyl ligand to Ni, which is often observed in the oxidized form, did not correlate with the Ni-elimination, but with exposure time to O2. Ni-elimination from the active site of the standard [NiFe]hydrogenase upon oxidation by O2.,Nishikawa K, Mochida S, Hiromoto T, Shibata N, Higuchi Y J Inorg Biochem. 2017 Dec;177:435-437. doi: 10.1016/j.jinorgbio.2017.09.011. Epub, 2017 Sep 14. PMID:28967475 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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