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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