Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 57, Issue 11, Pages 2855-2858Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201712948
Keywords
biomimetic; hydride transfer; hydrogen activation; mono-iron hydrogenase; scaffold chelate
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Funding
- Robert A. Welch Foundation [F-1822]
- ACS Petroleum Research Fund [53542-DN13]
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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 facCNS(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.
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