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Mössbauer and computational investigation of a functional [NiFe] hydrogenase model complex

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

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Bill,  E.
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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

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

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Citation

Kochem, A., Bill, E., Neese, F., & van Gastel, M. (2015). Mössbauer and computational investigation of a functional [NiFe] hydrogenase model complex. Chemical Communications, 51(11), 2099-2102. doi:10.1039/c4cc09035g.


Cite as: https://hdl.handle.net/21.11116/0000-0007-895A-A
Abstract
Developing biomimetic complexes that model the active site of [NiFe] hydrogenase enzymes in order to catalyze the activation of H2 is a topic of major interest. A functional [NiFe] hydrogenase model complex has recently been described by Ogo et al. (Science, 2013, 339, 682–683). Here, we report a Mössbauer and computational investigation of this model complex. This study affords deeper understanding of the electronic structure, the reactivity and the mechanism of H2 activation by this complex.