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, 57 Fe Mössbauer spectroscopy and SQUID magnetometry. Further, cleavage of the [Fe-S-Fe] unit by CS2 is presented.
Keywords: 57Fe Mössbauer spectroscopy; electrochemistry; iron sulfide complex; magnetism; nitrogenase.
© 2021 The Authors. Published by Wiley-VCH GmbH.