Toward Functional Type III [Fe]‐Hydrogenase Biomimics for H2 Activation: Insights from Computation |
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| Authors: | Kevin A Murray Dr Matthew D Wodrich Prof?Dr Xile Hu Prof?Dr Clémence Corminboeuf |
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| Affiliation: | 1. Laboratory for Computational Molecular Design, Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland);2. Laboratory of Inorganic Synthesis and Catalysis, Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland) |
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| Abstract: | The chemistry of Fe]‐hydrogenase has attracted significant interest due to its ability to activate molecular hydrogen. The intriguing properties of this enzyme have prompted the synthesis of numerous small molecule mimics aimed at activating H2. Despite considerable effort, a majority of these compounds remain nonfunctional for hydrogenation reactions. By using a recently synthesized model as an entry point, seven biomimetic complexes have been examined through DFT computations to probe the influence of ligand environment on the ability of a mimic to bind and split H2. One mimic, featuring a bidentate diphosphine group incorporating an internal nitrogen base, was found to have particularly attractive energetics, prompting a study of the role played by the proton/hydride acceptor necessary to complete the catalytic cycle. Computations revealed an experimentally accessible energetic pathway involving a benzaldehyde proton/hydride acceptor and the most promising catalyst. |
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| Keywords: | biomimetic chemistry density functional calculations enzyme models hydrogenase ligand effects |
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