1391711-48-0Relevant articles and documents
Ammonia formation by a thiolate-bridged diiron amide complex as a nitrogenase mimic
Li, Yang,Li, Ying,Wang, Baomin,Luo, Yi,Yang, Dawei,Tong, Peng,Zhao, Jinfeng,Luo, Lun,Zhou, Yuhan,Chen, Si,Cheng, Fang,Qu, Jingping
, p. 320 - 326 (2013)
Although nitrogenase enzymes routinely convert molecular nitrogen into ammonia under ambient temperature and pressure, this reaction is currently carried out industrially using the Haber-Bosch process, which requires extreme temperatures and pressures to activate dinitrogen. Biological fixation occurs through dinitrogen and reduced NxHy species at multi-iron centres of compounds bearing sulfur ligands, but it is difficult to elucidate the mechanistic details and to obtain stable model intermediate complexes for further investigation. Metal-based synthetic models have been applied to reveal partial details, although most models involve a mononuclear system. Here, we report a diiron complex bridged by a bidentate thiolate ligand that can accommodate HN=NH. Following reductions and protonations, HN=NH is converted to NH 3 through pivotal intermediate complexes bridged by N2H 3- and NH2- species. Notably, the final ammonia release was effected with water as the proton source. Density functional theory calculations were carried out, and a pathway of biological nitrogen fixation is proposed.
