Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments
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.
- Authors:
-
- Univ. of California, Irvine, CA (United States)
- Publication Date:
- Research Org.:
- Univ. of California, Irvine, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1533142
- Alternate Identifier(s):
- OSTI ID: 1375467
- Grant/Contract Number:
- SC0014470
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Chemistry - A European Journal
- Additional Journal Information:
- Journal Volume: 23; Journal Issue: 51; Journal ID: ISSN 0947-6539
- Publisher:
- ChemPubSoc Europe
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Chemistry
Citation Formats
Sickerman, Nathaniel S., Tanifuji, Kazuki, Hu, Yilin, and Ribbe, Markus W. Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments. United States: N. p., 2017.
Web. doi:10.1002/chem.201702496.
Sickerman, Nathaniel S., Tanifuji, Kazuki, Hu, Yilin, & Ribbe, Markus W. Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments. United States. https://doi.org/10.1002/chem.201702496
Sickerman, Nathaniel S., Tanifuji, Kazuki, Hu, Yilin, and Ribbe, Markus W. Thu .
"Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments". United States. https://doi.org/10.1002/chem.201702496. https://www.osti.gov/servlets/purl/1533142.
@article{osti_1533142,
title = {Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments},
author = {Sickerman, Nathaniel S. and Tanifuji, Kazuki and Hu, Yilin and Ribbe, Markus W.},
abstractNote = {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},
journal = {Chemistry - A European Journal},
number = 51,
volume = 23,
place = {United States},
year = {Thu Jul 20 00:00:00 EDT 2017},
month = {Thu Jul 20 00:00:00 EDT 2017}
}
Web of Science
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- Hozumi, Yoshiyuki; Imasaka, Yoshinobu; Tanaka, Koji
- Chemistry Letters, Vol. 12, Issue 6
Structural Characterization and Reactivity Properties of a New Class of Fe/Mo/S Double Cubanes with Mo-Bound S-.mu.2-.eta.1,O-.eta.1 Mercapto Carboxylate Ligands. New Catalysts for the Reduction of Hydrazine to Ammonia and Implications Regarding the Function of Nitrogenase
journal, July 1995
- Demadis, Konstantinos D.; Coucouvanis, Dimitri
- Inorganic Chemistry, Vol. 34, Issue 14
Works referencing / citing this record:
A Comparative Analysis of the CO-Reducing Activities of MoFe Proteins Containing Mo- and V-Nitrogenase Cofactors
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N 2 Reduction on Fe‐Based Complexes with Different Supporting Main‐Group Elements: Critical Roles of Anchor and Peripheral Ligands
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Comparison of hydroxycarboxylato imidazole molybdenum( iv ) complexes and nitrogenase protein structures: indirect evidence for the protonation of homocitrato FeMo-cofactors
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- Wang, Si-Yuan; Jin, Wan-Ting; Chen, Hong-Bin
- Dalton Transactions, Vol. 47, Issue 22
Synthesis and reactivity of asymmetric Cr( i ) dinitrogen complexes supported by cyclopentadienyl–phosphine ligands
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A Cu/Zn heterometallic complex with solvent-binding cavity, catalytic activity for the oxidation of 1-phenylethanol and unusual magnetic properties
journal, January 2019
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Steric Switching From Photochemical to Thermal N2 Splitting: A Computational Analysis of the Isomerization Reaction {(Cp*)(Am)Mo}2(μ-η1:η1-N2) → {(Cp*)(Am)Mo}2(μ-N)2
journal, May 2019
- Krewald, Vera
- Frontiers in Chemistry, Vol. 7