Electronic Structure of an [FeFe] Hydrogenase Model Complex in Solution Revealed by X-ray Absorption Spectroscopy Using Narrow-Band Emission Detection.

High-resolution X-ray absorption spectroscopy with narrow-band X-ray emission detection, supported by density functional theory calculations (XAES-DFT), was used to study a model complex, ([Fe(μ-adt)(CO)(PMe)] (1, adt = S-CH-(NCHPh)-CH-S), of the [FeFe] hydrogenase active site. For 1 in powder mater...

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Publicado en:Journal of the American Chemical Society Vol. 134; no. 34; pp. 14142 - 14158
Autores principales: Leidel, Nils, Chernev, Petko, Havelius, Kajsa G. V., Schwartz, Lennart, Ott, Sascha, Haumann, Michael
Formato: Artículo
Publicado: American Chemical Society 8/29/2012
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Acceso en línea:Ver este registro en EBSCOhost
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      dt: 8/29/2012
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      pub: American Chemical Society
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        10.1021/ja304970p
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        atl: Electronic Structure of an [FeFe] Hydrogenase Model Complex in Solution Revealed by X-ray Absorption Spectroscopy Using Narrow-Band Emission Detection.
      aug:
        au:
          Leidel, Nils
          Chernev, Petko
          Havelius, Kajsa G. V.
          Schwartz, Lennart
          Ott, Sascha
          Haumann, Michael
        affil:
          Institut für Experimentalphysik, Freie Universität Berlin, 14195 Berlin, Germany
          Department of Chemistry, Uppsala University, Ångström Laboratories, 75120 Uppsala, Sweden
      su:
        Quantum chemistry
        Density functionals
        Solution (Chemistry)
        Hydrogen-ion concentration
        Molecular orbitals
        Chemical inhibitors
        Molecular structure
      sug:
        subj:
          Quantum chemistry
          Density functionals
          Solution (Chemistry)
          Hydrogen-ion concentration
          Molecular orbitals
          Chemical inhibitors
          Molecular structure
      ab: High-resolution X-ray absorption spectroscopy with narrow-band X-ray emission detection, supported by density functional theory calculations (XAES-DFT), was used to study a model complex, ([Fe(μ-adt)(CO)(PMe)] (1, adt = S-CH-(NCHPh)-CH-S), of the [FeFe] hydrogenase active site. For 1 in powder material (1), in MeCN solution (1′), and in its three protonated states (1H, 1Hy, 1HHy; H denotes protonation at the adt-N and Hy protonation of the Fe-Fe bond to form a bridging metal hydride), relations between the molecular structures and the electronic configurations were determined. EXAFS analysis and DFT geometry optimization suggested prevailing rotational isomers in MeCN, which were similar to the crystal structure or exhibited rotation of the (CO) ligands at Fe1 (1, 1Hy) and in addition of the phenyl ring (1H, 1HHy), leading to an elongated solvent-exposed Fe-Fe bond. Isomer formation, adt-N protonation, and hydride binding caused spectral changes of core-to-valence (pre-edge of the Fe K-shell absorption) and of valence-to-core (Kß2,5 emission) electronic transitions, and of Kα RIXS data, which were quantitatively reproduced by DFT. The study reveals (1) the composition of molecular orbitals, for example, with dominant Fe-d character, showing variations in symmetry and apparent oxidation state at the two Fe ions and a drop in MO energies by ~1 eV upon each protonation step, (2) the HOMO-LUMO energy gaps, of ~2.3 eV for 1 and ~2.0 eV for 1′, and (3) the splitting between iron d(z) and d(x-y) levels of ~0.5 eV for the nonhydride and ~0.9 eV for the hydride states. Good correlations of reduction potentials to LUMO energies and oxidation potentials to HOMO energies were obtained. Two routes of facilitated bridging hydride binding thereby are suggested, involving ligand rotation at Fe1 for 1Hy or adt-N protonation for 1HHy. XAES-DFT thus enables verification of the effects of ligand substitutions in solution for guided improvement of [FeFe] catalysts.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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          year: 2012
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