Vela Javier, Stoian Sebastian, Flaschenriem Christine J, Münck Eckard, Holland Patrick L
Department of Chemistry, University of Rochester, Rochester, New York 14627, USA.
J Am Chem Soc. 2004 Apr 14;126(14):4522-3. doi: 10.1021/ja049417l.
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).
固氮酶的活性位点铁钼辅因子含有由硫化物桥连的、具有氧化还原活性的三角锥型铁原子对,据推测这是N₂转化的位点。本文描述了一种合成化合物,其中两个三配位铁(II)离子通过硫化物以类似方式桥连。该化合物能结合氮供体形成三角锥构型,并在铁(II)氧化为铁(III)的过程中裂解苯肼的N-N键。