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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
Functional Hydride Transfer by a Thiolate-Containing Model of Mono-Iron Hydrogenase featuring an Anthracene Scaffold
Spencer A Kerns1, Anne-Clarisse Magtaan1, Pisey R Vong1
1Department of Chemistry, The University of Texas at Austin, Austin, TX, 78712, USA.
Abstract:
We report the synthesis, X-ray structure and functional biomimetic activity of a model complex of mono-iron hydrogenase (Hmd). To achieve the desired biomimetic fac-CNS(thiolate) ligation motif, an anthracene framework is used to provide the requisite donors in a single chelate. A bulky aryl thiolate (ortho dimethylphenyl) is included to achieve mononuclearity. In addition to exhibiting structural (X-ray) and spectroscopic (NMR, IR) similarity to the enzyme, the complex is competent for H2 activation (heterolysis) and hydride transfer to a model substrate-mimicking the functional behavior of the enzyme in a biomimetic CNS coordination sphere for the first time.
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