In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 78, No. 2 ( 2022-02-01), p. 66-74
Abstract:
Hydrogenases catalyze the reversible oxidation of H 2 . Carbon monoxide (CO) is known to be a competitive inhibitor of O 2 -sensitive [NiFe]-hydrogenases. Although the activities of some O 2 -tolerant [NiFe]-hydrogenases are unaffected by CO, the partially O 2 -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 2+ 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 2 and CO tolerance in [NiFe]-hydrogenases.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X22000188
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2022
detail.hit.zdb_id:
2175956-X