Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase

Marine Bacchi, Elias Veinberg, Martin J. Field, Jens Niklas, Toshitaka Matsui, D. M. Tiede, Oleg G. Poluektov, Masao Ikeda-Saito, Marc Fontecave, Vincent Artero

研究成果: Article査読

11 被引用数 (Scopus)

抄録

The insertion of cobaloxime catalysts in the heme-binding pocket of heme oxygenase (HO) yields artificial hydrogenases active for H2 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} (dmgH2=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.

本文言語English
ページ(範囲)1083-1089
ページ数7
ジャーナルChemPlusChem
81
10
DOI
出版ステータスPublished - 2016 10 1

ASJC Scopus subject areas

  • Chemistry(all)

フィンガープリント 「Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル