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. 2018 Mar 5;57(11):2855-2858.
doi: 10.1002/anie.201712948. Epub 2018 Feb 14.

Functional Hydride Transfer by a Thiolate-Containing Model of Mono-Iron Hydrogenase Featuring an Anthracene Scaffold

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Functional Hydride Transfer by a Thiolate-Containing Model of Mono-Iron Hydrogenase Featuring an Anthracene Scaffold

Spencer A Kerns et al. Angew Chem Int Ed Engl. .

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.

Keywords: biomimetic; hydride transfer; hydrogen activation; mono-iron hydrogenase; scaffold chelate.

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