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[FeFe]-Hydrogenase H-cluster mimics mediated by naphthalene monoimide derivatives of peri-substituted dichalcogenides

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Abstract

Synthetic models of the active site of [FeFe]-hydrogenase containing naphthalene monoimide (NMI) of peri-substituted dichalcogenides as bridging linkers have been prepared and characterized using different spectroscopic methods. The influence of the imide functionality and the chalcogen atoms on the redox properties and the catalytic behaviour of complexes 7–10 was studied using cyclic voltammetry. The results revealed that the imide functionality has improved the chemical stability of the reduced species and the replacement of the S atoms by Se caused a cathodic shift in the oxidation peaks. Moreover, the optical properties of compounds 1, 2, 4, and 5 and the respective diiron complexes 7–10 were investigated by UV-Vis absorption and fluorescence spectroscopy assisted by quantum chemical simulations. The structures of complexes 6–9 were confirmed by X-ray diffraction analysis.

Graphical abstract: [FeFe]-Hydrogenase H-cluster mimics mediated by naphthalene monoimide derivatives of peri-substituted dichalcogenides

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Publication details

The article was received on 07 Jun 2017, accepted on 24 Jun 2017 and first published on 26 Jun 2017


Article type: Paper
DOI: 10.1039/C7DT02079A
Citation: Dalton Trans., 2017, Advance Article
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    [FeFe]-Hydrogenase H-cluster mimics mediated by naphthalene monoimide derivatives of peri-substituted dichalcogenides

    H. Abul-Futouh, Y. Zagranyarski, C. Müller, M. Schulz, S. Kupfer, H. Görls, M. El-khateeb, S. Gräfe, B. Dietzek, K. Peneva and W. Weigand, Dalton Trans., 2017, Advance Article , DOI: 10.1039/C7DT02079A

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