7VXQ
The Carbon Monoxide Complex of [NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77
Summary for 7VXQ
| Entry DOI | 10.2210/pdb7vxq/pdb |
| Descriptor | [NiFe]-hydrogenase 2 large subunit, NiFe hydrogenase, MAGNESIUM ION, ... (9 entities in total) |
| Functional Keywords | [nife] hydrogenase, oxidoreductase |
| Biological source | Citrobacter sp. S-77 More |
| Total number of polymer chains | 4 |
| Total formula weight | 196433.93 |
| Authors | Nishikawa, K.,Higuchi, K.,Imanishi, T.,Higuchi, Y. (deposition date: 2021-11-13, release date: 2022-02-09, Last modification date: 2023-11-29) |
| Primary citation | Imanishi, T.,Nishikawa, K.,Taketa, M.,Higuchi, K.,Tai, H.,Hirota, S.,Hojo, H.,Kawakami, T.,Hataguchi, K.,Matsumoto, K.,Ogata, H.,Higuchi, Y. Structural and spectroscopic characterization of CO inhibition of [NiFe]-hydrogenase from Citrobacter sp. S-77. Acta Crystallogr.,Sect.F, 78:66-74, 2022 Cited by PubMed Abstract: Hydrogenases catalyze the reversible oxidation of H. Carbon monoxide (CO) is known to be a competitive inhibitor of O-sensitive [NiFe]-hydrogenases. Although the activities of some O-tolerant [NiFe]-hydrogenases are unaffected by CO, the partially O-tolerant [NiFe]-hydrogenase from Citrobacter sp. S-77 (S77-HYB) is inhibited by CO. In this work, the CO-bound state of S77-HYB was characterized by activity assays, spectroscopic techniques and X-ray crystallography. Electron paramagnetic resonance spectroscopy showed a diamagnetic Ni state, and Fourier-transform infrared spectroscopy revealed the stretching vibration of the exogenous CO ligand. The crystal structure determined at 1.77 Å resolution revealed that CO binds weakly to the nickel ion in the Ni-Fe active site of S77-HYB. These results suggest a positive correlation between O and CO tolerance in [NiFe]-hydrogenases. PubMed: 35102895DOI: 10.1107/S2053230X22000188 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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