Electron delocalization from the fullerene attachment to the diiron core within the active-site mimics of [FeFe]hydrogenase

Inorg Chem. 2012 Jun 4;51(11):5997-9. doi: 10.1021/ic3007298. Epub 2012 May 16.


Attachment of the redox-active C(60)(H)PPh(2) group modulates the electronic structure of the Fe(2) core in [(μ-bdt)Fe(2)(CO)(5)(C(60)(H)PPh(2))]. The neutral complex is characterized by X-ray crystallography, IR, NMR spectroscopy, and cyclic voltammetry. When it is reduced by one electron, the spectroscopic and density functional theory results indicate that the Fe(2) core is partially spin-populated. In the doubly reduced species, extensive electron communication occurs between the reduced fullerene unit and the Fe(2) centers as displayed in the spin-density plot. The results suggest that the [4Fe4S] cluster within the H cluster provides an essential role in terms of the electronic factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomimetic Materials / chemistry*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Electrons
  • Fullerenes / chemistry*
  • Hydrogenase / chemistry*
  • Iron / chemistry*
  • Iron-Sulfur Proteins / chemistry*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Oxidation-Reduction


  • Fullerenes
  • Iron-Sulfur Proteins
  • Iron
  • Hydrogenase