Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 27, Issue 20, Pages 6348-6353Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202100336
Keywords
Fe-57 Mö ssbauer spectroscopy; electrochemistry; iron sulfide complex; magnetism; nitrogenase
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [WE 5627/4-1, Me 1313/13-2]
- Projekt DEAL
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This study reports a dinuclear monosulfido bridged diiron(II) complex with a similar [Fe-S-Fe] core geometry that can be stepwise oxidized to different oxidation states while retaining the core structure. The cleavage of the [Fe-S-Fe] unit by CS2 is also demonstrated in this research. The complexes have been characterized crystallographically and electron structures have been studied using various techniques such as Fe-57 Mossbauer spectroscopy and SQUID magnetometry.
A [Fe-S-Fe] subunit with a single sulfide bridging two low-coordinate iron ions is the supposed active site of the iron-molybdenum co-factor (FeMoco) of nitrogenase. Here we report a dinuclear monosulfido bridged diiron(II) complex with a similar complex geometry that can be oxidized stepwise to diiron(II/III) and diiron(III/III) complexes while retaining the [Fe-S-Fe] core. The series of complexes has been characterized crystallographically, and electronic structures have been studied using, inter alia, Fe-57 Mossbauer spectroscopy and SQUID magnetometry. Further, cleavage of the [Fe-S-Fe] unit by CS2 is presented.
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