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Literature summary for 1.18.6.1 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
Search for more literature for 1.18.6.1

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
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-
-

Cofactor

Cofactor Comment Organism Structure
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

General Information Comment Organism
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