A sulfido-bridged diiron(II) compound and its reactions with nitrogenase-relevant substrates.
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).
Vela
Javier
J
Department of Chemistry, University of Rochester, Rochester, New York 14627, USA.
Stoian
Sebastian
S
Flaschenriem
Christine J
CJ
Münck
Eckard
E
Holland
Patrick L
PL
D005296:Ferrous Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D008983:Molybdoferredoxin / Q000737:chemistry*; D009591:Nitrogenase / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D013440:Sulfides / Q000138:chemical synthesis / Q000737:chemistry*
D005296:Ferrous Compounds; D008983:Molybdoferredoxin; D013440:Sulfides; D009591:Nitrogenase