Nitrogenase Cofactor: Inspiration for Model Chemistry

Djurdjević, Ivana; Einsle, Oliver; Decamps, Laure

doi:10.1002/asia.201700478

Cited by 25 publications

(16 citation statements)

References 67 publications

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“…It is present at nitrogenase's active site and is recognized for its unique catalytic solution to reduce N 2 to NH 3 . However, FeMo-co extracted from nitrogenase into organic solvents cannot directly catalyze the reduction of N 2 to NH 3 due to the crucial influence of the protein matrix on its reactivity [93]. Therefore, the use of compounds such as Mo sources that act as ligands and redox reagents is significant for successfully synthesizing FeMo-co analogues whose stability and isolation are dependent on steric bulky groups of these donor ligands [52,94].…”

Section: Structure Of Femo-comentioning

confidence: 99%

Progress in Synthesizing Analogues of Nitrogenase Metalloclusters for Catalytic Reduction of Nitrogen to Ammonia

Yang

2019

Catalysts

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Ammonia (NH3) has played an essential role in meeting the increasing demand for food and the worldwide need for nitrogen (N2) fertilizer since 1913. Unfortunately, the traditional Haber–Bosch process for producing NH3 from N2 is a high energy-consumption process with approximately 1.9 metric tons of fossil CO2 being released per metric ton of NH3 produced. As a very challenging target, any ideal NH3 production process reducing fossil energy consumption and environmental pollution would be welcomed. Catalytic NH3 synthesis is an attractive and promising alternative approach. Therefore, developing efficient catalysts for synthesizing NH3 from N2 under ambient conditions would create a significant opportunity to directly provide nitrogenous fertilizers in agricultural fields as needed in a distributed manner. In this paper, the literature on alternative, available, and sustainable NH3 production processes in terms of the scientific aspects of the spatial structures of nitrogenase metalloclusters, the mechanism of reducing N2 to NH3 catalyzed by nitrogenase, the synthetic analogues of nitrogenase metalloclusters, and the opportunities for continued research are reviewed.

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Section: Structure Of Femo-comentioning

confidence: 99%

Progress in Synthesizing Analogues of Nitrogenase Metalloclusters for Catalytic Reduction of Nitrogen to Ammonia

Yang

2019

Catalysts

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“…Tremendous progress in understanding biological dinitrogen fixation was made in recent years . Among other things, the key steps for the maturation of the sophisticated metallocenters have been deciphered, which might be an important step towards the design of plants or plant‐associated organisms with improved nitrogen‐fixing ability.…”

Section: Introductionmentioning

confidence: 99%

Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase

et al. 2020

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The engineering of transgenic organisms with the ability to fix nitrogen is an attractive possibility. However, oxygen sensitivity of nitrogenase, mainly conferred by the reductase component (NifH)2, is an imminent problem. Nitrogenase‐like enzymes involved in coenzyme F430 and chlorophyll biosynthesis utilize the highly homologous reductases (CfbC)2 and (ChlL)2, respectively. Chimeric protein–protein interactions of these reductases with the catalytic component of nitrogenase (MoFe protein) did not support nitrogenase activity. Nucleotide‐dependent association and dissociation of these complexes was investigated, but (CfbC)2 and wild‐type (ChlL)2 showed no modulation of the binding affinity. By contrast, the interaction between the (ChlL)2 mutant Y127S and the MoFe protein was markedly increased in the presence of ATP (or ATP analogues) and reduced in the ADP state. Upon formation of the octameric (ChlL)2MoFe(ChlL)2 complex, the ATPase activity of this variant is triggered, as seen in the homologous nitrogenase system. Thus, the described reductase(s) might be an attractive tool for further elucidation of the diverse functions of (NifH)2 and the rational design of a more robust reductase.

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“…[1][2][3][4] The development of this field is linked to the problems raised by nitrogen fixation into the biosphere : indeed, dinitrogen complexes have proven valuable models in order to understand the functioning of the nitrogenases. [5][6][7] Besides, the environmental and sustainability concerns linked to anthropogenic N fixation via the Haber-Bosch process [8][9][10][11] have fueled a quest for bio-inspired molecular alternatives. [12][13][14][15] Among all the dinitrogen complexes found in the literature, a very common coordination mode is the terminal one.…”

Section: Introductionmentioning

confidence: 99%