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A sulfido-bridged diiron(II) compound and its reactions with nitrogenase-relevant substrates
Javier Vela1, Sebastian Stoian, Christine J Flaschenriem
1Department of Chemistry, University of Rochester, Rochester, New York 14627, USA.
Abstract:
The active site iron-molybdenum cofactor of nitrogenase has sulfide-bridged pairs of redox-active, trigonal pyramidal iron atoms that are postulated to be the site of N2 transformation. A synthetic compound is described in which two three-coordinate iron(II) ions are bridged similarly by sulfide. The compound binds nitrogen donors to become trigonal pyramidal and cleaves the N-N bond of phenylhydrazine with oxidation of iron(II) to iron(III).
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