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  • Title: Heterolytic cleavage of hydrogen by an iron hydrogenase model: an Fe-H⋅⋅⋅H-N dihydrogen bond characterized by neutron diffraction.
    Author: Liu T, Wang X, Hoffmann C, DuBois DL, Bullock RM.
    Journal: Angew Chem Int Ed Engl; 2014 May 19; 53(21):5300-4. PubMed ID: 24757087.
    Abstract:
    Hydrogenase enzymes in nature use hydrogen as a fuel, but the heterolytic cleavage of H-H bonds cannot be readily observed in enzymes. Here we show that an iron complex with pendant amines in the diphosphine ligand cleaves hydrogen heterolytically. The product has a strong Fe-H⋅⋅⋅H-N dihydrogen bond. The structure was determined by single-crystal neutron diffraction, and has a remarkably short H⋅⋅⋅H distance of 1.489(10) Å between the protic N-H(δ+) and hydridic Fe-H(δ-) part. The structural data for [Cp(C5F4N)FeH(P(tBu)2N(tBu)2H)](+) provide a glimpse of how the H-H bond is oxidized or generated in hydrogenase enzymes. These results now provide a full picture for the first time, illustrating structures and reactivity of the dihydrogen complex and the product of the heterolytic cleavage of H2 in a functional model of the active site of the [FeFe] hydrogenase enzyme.
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