Service interruption on Monday 11 July from 12:30 to 13:00: all the sites of the CCSD (HAL, Epiciences, SciencesConf, AureHAL) will be inaccessible (network hardware connection).
Skip to Main content Skip to Navigation
Journal articles

Mechanism of inhibition of NiFe hydrogenase by nitric oxide

Abstract : Hydrogenases reversibly catalyze the oxidation of molecular hydrogen and are inhibited by several small molecules including O2, CO and NO. In the present work, we investigate the mechanism of inhibition by NO of the oxygen-sensitive NiFe hydrogenase from Desulfovibrio fructosovorans by coupling site-directed mutagenesis, protein film voltammetry (PFV) and EPR spectroscopy. We show that micromolar NO strongly inhibits NiFe hydrogenase and that the mechanism of inhibition is complex, with NO targeting several metallic sites in the protein. NO reacts readily at the NiFe active site according to a two-step mechanism. The first and faster step is the reversible binding of NO to the active site followed by a slower and irreversible transformation at the active site. NO also induces irreversible damage of the iron–sulfur centers chain. We give direct evidence of preferential nitrosylation of the medial [3Fe–4S] to form dinitrosyl–iron complexes.
Document type :
Journal articles
Complete list of metadata
Contributor : LAURE AZZOPARDI Connect in order to contact the contributor
Submitted on : Friday, December 9, 2016 - 2:41:35 PM
Last modification on : Wednesday, November 3, 2021 - 4:05:54 AM

Links full text




Pierre Ceccaldi, Emilien Etienne, Sébastien Dementin, Bruno Guigliarelli, Christophe Léger, et al.. Mechanism of inhibition of NiFe hydrogenase by nitric oxide. Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, Elsevier, 2016, Volume 1857, Issue 4 (1857), pp.454-461. ⟨10.1016/j.bbabio.2016.01.014⟩. ⟨hal-01413192⟩



Record views