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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
Impact of Secondary Sphere Hydrogen Bonds on O2 Reactivity within a Nonheme Iron Complex
Andrew R LaDuca1, Jessica R Wilson1, Writhabrata Sarkar1
1Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States.
Abstract:
A nonheme iron complex bearing the tris(6-phenylamino-pyridyl)methylamine (TPANHPh) ligand with appended hydrogen bond (H-bond) groups displays facile O2 reactivity to form a monomeric Fe(III)OH complex, which can release •OH via rebound to a carbon radical. An analogous compound without H-bonds, based on tris(6-methylpyridyl)methylamine (TPAMe), exhibits minimal O2 reactivity, forming a Fe(III)2(μ-O)(μ-OH) dimer, which also reacts with carbon-based radicals. The H-bonding system enables O2 binding and activation at weakly reducing nonheme iron complexes, highlighting a cooperative role of secondary sphere units to facilitate reactions at atypical redox environments.
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