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Issue 34, 2017
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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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Supplementary files

Article information


Submitted
07 Jun 2017
Accepted
24 Jun 2017
First published
26 Jun 2017

Dalton Trans., 2017,46, 11180-11191
Article type
Paper

[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, 46, 11180
DOI: 10.1039/C7DT02079A

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