7VXQ

The Carbon Monoxide Complex of [NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77

7VXQ の概要

• エントリーDOI: 10.2210/pdb7vxq/pdb
• 分子名称: [NiFe]-hydrogenase 2 large subunit, NiFe hydrogenase, MAGNESIUM ION, ... (9 entities in total)
• 機能のキーワード: [nife] hydrogenase, oxidoreductase
• 由来する生物種: Citrobacter sp. S-77; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 196433.93

構造登録者

Nishikawa, K.,Higuchi, K.,Imanishi, T.,Higuchi, Y. (登録日: 2021-11-13, 公開日: 2022-02-09, 最終更新日: 2023-11-29)

主引用文献

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

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: 35102895
DOI: 10.1107/S2053230X22000188

実験手法

X-RAY DIFFRACTION (1.77 Å)