CO and CN- syntheses by [FeFe]-hydrogenase maturase HydG are catalytically differentiated events. - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2016

CO and CN- syntheses by [FeFe]-hydrogenase maturase HydG are catalytically differentiated events.

Résumé

The synthesis and assembly of the active site [FeFe] unit of [FeFe]-hydrogenases require at least three maturases. The radical S-adenosyl-l-methionine HydG, the best characterized of these proteins, is responsible for the synthesis of the hydrogenase CO and CN(-) ligands from tyrosine-derived dehydroglycine (DHG). We speculated that CN(-) and the CO precursor (-):CO2H may be generated through an elimination reaction. We tested this hypothesis with both wild type and HydG variants defective in second iron-sulfur cluster coordination by measuring the in vitro production of CO, CN(-), and (-):CO2H-derived formate. We indeed observed formate production under these conditions. We conclude that HydG is a multifunctional enzyme that produces DHG, CN(-), and CO at three well-differentiated catalytic sites. We also speculate that homocysteine, cysteine, or a related ligand could be involved in Fe(CO)x(CN)y transfer to the HydF carrier/scaffold.
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Dates et versions

hal-01252697 , version 1 (08-01-2016)

Identifiants

  • HAL Id : hal-01252697 , version 1
  • PUBMED : 26699472

Citer

Adrien Pagnier, Lydie Martin, Laura Zeppieri, Yvain Nicolet, Juan-Carlos Fontecilla-Camps. CO and CN- syntheses by [FeFe]-hydrogenase maturase HydG are catalytically differentiated events.. Proceedings of the National Academy of Sciences of the United States of America, 2016, 113 (1), pp.104-9. ⟨hal-01252697⟩
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