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Article Dans Une Revue ChemPlusChem Année : 2016

Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase

Résumé

The insertion of cobaloxime catalysts in the heme-binding pocket of heme oxygenase (HO) yields artificial hydrogenases active for H-2 evolution in neutral aqueous solutions. These novel biohybrids have been purified and characterized by using UV/visible and EPR spectroscopy. These analyses revealed the presence of two distinct binding conformations, thereby providing the cobaloxime with hydrophobic and hydrophilic environments, respectively. Quantum chemical/molecular mechanical docking calculations found open and closed conformations of the binding pocket owing to mobile amino acid residues. HO-based biohybrids incorporating a {Co(dmgH)(2)} (dmgH(2)=dimethylglyoxime) catalytic center displayed up to threefold increased turnover numbers with respect to the cobaloxime alone or to analogous sperm whale myoglobin adducts. This study thus provides a strong basis for further improvement of such biohybrids, using well-designed modifications of the second and outer coordination spheres, through site-directed mutagenesis of the host protein.

Domaines

Chimie Catalyse

Dates et versions

hal-01437557 , version 1 (17-01-2017)

Identifiants

Citer

Marine Bacchi, Elias Veinberg, Martin J Field, Jens Niklas, Toshitaka Matsui, et al.. Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase. ChemPlusChem, 2016, 81 (10 Spécial issue), pp.1083-1089. ⟨10.1002/cplu.201600218⟩. ⟨hal-01437557⟩
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