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EPR and Quantum Chemical Investigation of a Bioinspired Hydrogenase Model with a Redox-Active Ligand in the First Coordination Sphere

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Kochem,  Amélie
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Weyhermüller,  Thomas
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Neese,  Frank
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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van Gastel,  Maurice
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Kochem, A., Weyhermüller, T., Neese, F., & van Gastel, M. (2015). EPR and Quantum Chemical Investigation of a Bioinspired Hydrogenase Model with a Redox-Active Ligand in the First Coordination Sphere. Organometallics, 34(5), 995-1000. doi:10.1021/acs.organomet.5b00039.


Cite as: https://hdl.handle.net/21.11116/0000-0007-8954-0
Abstract
Developing biomimetic complexes that model the active site of hydrogenase metalloenzymes in order to catalyze the activation of H2 is a topic of major interest. Here we report an EPR and computational investigation of a new heteroleptic nickel complex model, with relevance for H2 production, bearing a P2N2 ligand with proton relay in the second coordination sphere and a redox-active ligand in the first coordination sphere.