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Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments
Author(s) -
Sickerman Nathaniel S.,
Tanifuji Kazuki,
Hu Yilin,
Ribbe Markus W.
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201702496
Subject(s) - nitrogenase , nitrogen fixation , sulfur , chemistry , nanotechnology , biochemical engineering , computational biology , nitrogen , combinatorial chemistry , biology , materials science , organic chemistry , engineering
Nitrogenase is the only known biological system capable of reducing N 2 to NH 3 , 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 N 2 . 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 N 2 to NH 3 , the insights borne from past and recent developments are discussed in this concept article.