A nitrogenase cluster model [Fe8S6O] with an oxygen unsymmetrically bridging two proto-Fe4S3 cubes: relevancy to the substrate binding mode of the FeMo cofactor

Inorg Chem. 2012 Nov 5;51(21):11217-9. doi: 10.1021/ic301348f. Epub 2012 Oct 25.


An oxygen-encapsulated iron sulfido cluster, [(DmpS)Fe(4)S(3)O][(DmpS)Fe(4)S(3)](μ-SDmp)(2)(μ-OCPh(3)) (2; Dmp = 2,6-(mesityl)(2)C(6)H(3)), has been synthesized by the reaction of the preformed dinuclear iron thiolate/alkoxide [(Ph(3)CO)Fe](2)(μ-SDmp)(2) (1) with (1/8)S(8) and (1/4)H(2)O in toluene. In the [Fe(8)S(6)O] core, the oxygen atom bridges unsymmetrically two incomplete Fe(4)S(3) cubes, and two coordinatively unsaturated iron atoms are weakly bound to mesityl rings. Relevance of the cluster structure of 2 to the nitrogenase FeMo cofactor and its substrate binding mode is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Iron Compounds / chemical synthesis
  • Iron Compounds / chemistry*
  • Models, Molecular
  • Molybdoferredoxin / chemistry*
  • Molybdoferredoxin / metabolism
  • Oxygen / chemistry*
  • Protein Binding
  • Sulfides / chemical synthesis
  • Sulfides / chemistry*


  • Iron Compounds
  • Molybdoferredoxin
  • Sulfides
  • Oxygen