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Literature summary extracted from

  • Kaiser, J.T.; Hu, Y.; Wiig, J.A.; Rees, D.C.; Ribbe, M.W.
    Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase (2011), Science, 331, 91-94.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron in the FeMo cofactor Azotobacter vinelandii
1.18.6.1 Molybdenum in the FeMo cofactor Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
-
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 FeMo cofactor NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview Azotobacter vinelandii

General Information

EC Number General Information Comment Organism
1.18.6.1 additional information NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview Azotobacter vinelandii