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NifEN: a versatile player in nitrogenase assembly, catalysis and evolution.

Yilin Hu1, Markus W Ribbe2,3

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Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|December 11, 2024
PubMed
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Nitrogenase component NifEN, homologous to NifDK, can reduce nitrogen (N₂) to ammonia (NH₃). This dual function in assembly and catalysis suggests NifEN

Keywords:
AssemblyCatalysisEvolutionL-clusterM-clusterNitrogenase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Evolutionary Biology

Background:

  • The nitrogenase enzyme complex (NifDK) is crucial for biological nitrogen fixation.
  • NifEN shares structural and sequence homology with NifDK, possessing similar metallocenters.
  • NifEN is primarily known for its role in synthesizing the nitrogenase cofactor.

Purpose of the Study:

  • To review recent studies on the nitrogenase component NifEN.
  • To highlight the functional versatility of NifEN in both cofactor assembly and catalysis.
  • To explore the implications of NifEN's capabilities for understanding nitrogenase evolution and engineering.

Main Methods:

  • Comparative analysis of NifEN and NifDK structures and functions.
  • Review of experimental studies demonstrating NifEN's catalytic activities.
  • Bioinformatic and evolutionary perspectives on nitrogenase components.

Main Results:

  • NifEN catalyzes the reduction of nitrogen (N₂) to ammonia (NH₃) under ambient conditions.
  • NifEN possesses a dual role in the biosynthesis of the nitrogenase cofactor and direct substrate reduction.
  • Structural and sequence homology indicates NifEN as a potential evolutionary precursor to NifDK.

Conclusions:

  • NifEN's ability to reduce N₂ to NH₃ positions it as a plausible ancient nitrogenase.
  • The dual function of NifEN provides a model for reconstructing nitrogenase variants.
  • Understanding NifEN's versatility aids in mechanistic investigations and heterologous nitrogenase synthesis.