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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
Medium spin FeIII regulating the peroxide selectivity in the heterogeneous oxygen reduction reaction of
Cheng-Han Tso1, Chih-Hung Hsu2, Jiali Wang1
1Department of Chemistry, National Taiwan University, Taipei 106319, Taiwan. haomingchen@ntu.edu.tw.
Abstract:
Hydrogen peroxide (H2O2) can be produced cleanly and sustainably using electrosynthesis from the oxygen reduction reaction (ORR) via a 2-electron pathway, as opposed to the conventional anthraquinone technique. However, the rational design protocols for promoting the peroxide selectivity of ORR catalysts are still inadequate. This work synthesized a series of medium FeIII complexes with tetra-amido macrocyclic ligands (Fe-TAMLs) using a simplified two-step procedure. A relationship between peroxide selectivity and the spin polarization of metal centers in these Fe-TAML complex ORR catalysts is revealed. Using X-ray absorption spectroscopy (XAS) and X-ray emission spectroscopy (XES), the spin polarization of metal centers in Fe-TAMLs regulated by the ligand modification was studied. We found that the nitro group-substituted ligand Fe-TAML complex was regulated by its spin-polarization and offered the highest spin state enhancing peroxide selectivity about 55% to 78%. An operando XAS study is employed to verify the stability of the oxidation states and the robustness of the coordination structures of the Fe-TAMLs.
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