| Literature DB >> 15070362 |
Javier Vela1, Sebastian Stoian, Christine J Flaschenriem, Eckard Münck, Patrick L Holland.
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).Entities:
Mesh:
Substances:
Year: 2004 PMID: 15070362 DOI: 10.1021/ja049417l
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419