title: Electron delocalization from the fullerene attachment to the diiron core within the active-site mimics of [FeFe]hydrogenase.
abstract: 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.
authors.affiliation: Institute of Chemistry, Academia Sinica, Nankang, Taipei 115, Taiwan.
authors.forename: Yu-Chiao
authors.initials: YC
authors.lastname: Liu
authors.forename: Tao-Hung
authors.initials: TH
authors.lastname: Yen
authors.forename: Yu-Jan
authors.initials: YJ
authors.lastname: Tseng
authors.forename: Ching-Han
authors.initials: CH
authors.lastname: Hu
authors.forename: Gene-Hsiang
authors.initials: GH
authors.lastname: Lee
authors.forename: Ming-Hsi
authors.initials: MH
authors.lastname: Chiang
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004583:Electrons; D037741:Fullerenes / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010084:Oxidation-Reduction
chemical_list: D037741:Fullerenes; D007506:Iron-Sulfur Proteins; D007501:Iron; D006864:Hydrogenase