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Functional Hydride Transfer by a Thiolate‐Containing Model of Mono‐Iron Hydrogenase featuring an Anthracene Scaffold
Author(s) -
Kerns Spencer A.,
Magtaan AnneClarisse,
Vong Pisey R.,
Rose Michael J.
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201712948
Subject(s) - heterolysis , anthracene , hydride , chemistry , hydrogenase , combinatorial chemistry , electron transfer , enzyme , stereochemistry , photochemistry , organic chemistry , catalysis , metal
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 H 2 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.