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Updated: Nov 1, 2025
![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
Characterization and reactivity study of non-heme high-valent iron-hydroxo complexes
Kritika Keshari1, Moumita Bera1, Lucía Velasco2
1Department of Chemistry, Indian Institute of Technology Delhi Hauz Khas New Delhi 110016 India sparia@chemistry.iitd.ac.in.
Abstract:
A terminal FeIIIOH complex, [FeIII(L)(OH)]2- (1), has been synthesized and structurally characterized (H4L = 1,2-bis(2-hydroxy-2-methylpropanamido)benzene). The oxidation reaction of 1 with one equiv. of tris(4-bromophenyl)ammoniumyl hexachloroantimonate (TBAH) or ceric ammonium nitrate (CAN) in acetonitrile at -45 °C results in the formation of a FeIIIOH ligand radical complex, [FeIII(L˙)(OH)]- (2), which is hereby characterized by UV-visible, 1H nuclear magnetic resonance, electron paramagnetic resonance, and X-ray absorption spectroscopy techniques. The reaction of 2 with a triphenylcarbon radical further gives triphenylmethanol and mimics the so-called oxygen rebound step of Cpd II of cytochrome P450. Furthermore, the reaction of 2 was explored with different 4-substituted-2,6-di-tert-butylphenols. Based on kinetic analysis, a hydrogen atom transfer (HAT) mechanism has been established. A pK a value of 19.3 and a BDFE value of 78.2 kcal/mol have been estimated for complex 2.
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