title: Catalytic activation of H2 under mild conditions by an [FeFe]-hydrogenase model via an active μ-hydride species.
abstract: A [FeFe]-hydrogenase model (1) containing a chelating diphosphine ligand with a pendant amine was readily oxidized by Fc(+) (Fc = Cp2Fe) to a Fe(II)Fe(I) complex ([1](+)), which was isolated at room temperature. The structure of [1](+) with a semibridging CO and a vacant apical site was determined by X-ray crystallography. Complex [1](+) catalytically activates H2 at 1 atm at 25 °C in the presence of excess Fc(+) and P(o-tol)3. More interestingly, the catalytic activity of [1](+) for H2 oxidation remains unchanged in the presence of ca. 2% CO. A computational study of the reaction mechanism showed that the most favorable activation free energy involves a rotation of the bridging CO to an apical position followed by activation of H2 with the help of the internal amine to give a bridging hydride intermediate.
authors.affiliation: State Key Laboratory of Fine Chemicals, DUT-KTH Joint Education and Research Center on Molecular Devices, Dalian University of Technology (DUT), Dalian 116024, China.
authors.forename: Ning
authors.initials: N
authors.lastname: Wang
authors.forename: Mei
authors.initials: M
authors.lastname: Wang
authors.forename: Ying
authors.initials: Y
authors.lastname: Wang
authors.forename: Dehua
authors.initials: D
authors.lastname: Zheng
authors.forename: Hongxian
authors.initials: H
authors.lastname: Han
authors.forename: Mårten S G
authors.initials: MS
authors.lastname: Ahlquist
authors.forename: Licheng
authors.initials: L
authors.lastname: Sun
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D056831:Coordination Complexes / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006859:Hydrogen / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008958:Models, Molecular
chemical_list: D056831:Coordination Complexes; D007506:Iron-Sulfur Proteins; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase