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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Electron delocalization from the fullerene attachment to the diiron core within the active-site mimics of
Yu-Chiao Liu1, Tao-Hung Yen, Yu-Jan Tseng
1Institute of Chemistry, Academia Sinica, Nankang, Taipei 115, Taiwan.
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.
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