Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments
Sickerman, NS; Tanifuji, K; Hu, Y; Ribbe, MW
| HERO ID | 4736829 |
|---|---|
| In Press | No |
| Year | 2017 |
| Title | Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments |
| Authors | Sickerman, NS; Tanifuji, K; Hu, Y; Ribbe, MW |
| Journal | Chemistry: A European Journal |
| Volume | 23 |
| Issue | 51 |
| Page Numbers | 12425-12432 |
| Abstract | Nitrogenase is the only known biological system capable of reducing N2 to NH3 , which is a critical component of bioavailable nitrogen fixation. Since the discovery of discrete iron-sulfur metalloclusters within the nitrogenase MoFe protein, synthetic inorganic chemists have sought to reproduce the structural features of these clusters in order to understand how they facilitate the binding, activation and hydrogenation of N2 . Through the decades following the initial identification of these clusters, significant progress has been made to synthetically replicate certain compositional and functional aspects of the biogenic clusters. Although much work remains to generate synthetic iron-sulfur clusters that can reduce N2 to NH3 , the insights borne from past and recent developments are discussed in this concept article. |
| Doi | 10.1002/chem.201702496 |
| Pmid | 28726330 |
| Wosid | WOS:000410329100001 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |