期刊
DALTON TRANSACTIONS
卷 52, 期 27, 页码 9215-9228出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d3dt01285a
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In this study, a series of new structural and functional [Fe]-H(2)ase models were reported, showing enzyme-like H-2 activation and hydride transfer functions.
The combined structural and functional modeling study of [Fe]-H(2)ase has remained a great challenge, to date. Now, we report a series of new structural and functional [Fe]-H(2)ase models (1-6) that contain a mono-, di- or tetrasubstituted pyridine ligand with a biomimetic fac-C, N, and S ligation. While models 1-3, 5 and 6 are conveniently prepared by a novel flexible pyridine ligand (FPL)-based method, model 4 is prepared simply by an intramolecular CO replacement reaction of model 3. More interestingly, the structural study by spectroscopy and X-ray crystallography proves that these new models include a biomimetic fac-acyl (or methylene) C, pyridyl N, and thioether S ligation to an Fe(ii) center and the C-Fe(ii) s bond is trans to an iodo ligand. In addition, the chemical reactivity study proves that they all have the enzyme-like H-2 activation and hydride transfer functions in the presence of imidazolium Im(+), AgBF4 and Et3N. Particularly interesting is that a possible pathway for such H-2 activation and hydride transfer reactions catalyzed by a representative model 4 is proposed and the existence of the highly unstable 5-coordinate intermediate M-4 and Fe-H species M-5 is supported by the isolation and characterization of their MeCN-coordinated derivative 7 and chloro-substituted derivative 8, respectively.
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