Structural and Spectroscopic Characterization of CO Inhibition of [NiFe]-hydrogenase from Citrobacter Sp. S-77

Overview

Journal Acta Crystallogr F Struct Biol Commun

Specialty Chemistry

Date 2022 Feb 1

PMID 35102895

Authors

Takahiro Imanishi

Koji Nishikawa

Midori Taketa

Katsuhiro Higuchi

Hulin Tai

Shun Hirota

Hironobu Hojo

Toru Kawakami

Kiriko Hataguchi

Kayoko Matsumoto

Hideaki Ogata

Yoshiki Higuchi

Affiliations

Soon will be listed here.

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.

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