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Literature summary for 1.18.6.1 extracted from

  • Hu, Y.; Fay, A.W.; Lee, C.C.; Wiig, J.A.; Ribbe, M.W.
    Dual functions of NifEN: insights into the evolution and mechanism of nitrogenase (2010), Dalton Trans., 39, 2964-2971.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.6.1

Metals/Ions

Metals/Ions Comment Organism Structure
Fe molybdenum-iron protein component and an iron protein component with an iron-molybdenum cofactor center. Schematic structure of the alpha2-dimeric Fe protein, which contains a [Fe4S4] cluster at the subunit interface and an MgATP binding site within each subunit, overview Azotobacter vinelandii
Mg2+ MgATP2- is required Azotobacter vinelandii
Mo molybdenum-iron protein component with an iron-molybdenum cofactor center. Schematic structureof the alpha2beta2-tetrameric MoFe protein, which contains a pair of unique clusters in each ab-subunit dimer, the P-cluster ([Fe8S7]) at the alphabeta-subunit interface, and the FeMoco ([MoFe7S9X], where X=C,N, or O) within the alpha-subunit Azotobacter vinelandii
additional information structures of the metal centers in Fe protein and MoFe protein, overview Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Azotobacter vinelandii nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor ?
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Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor Azotobacter vinelandii ?
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Subunits

Subunits Comment Organism
More components of the electron transfer chains in nitrogenase and its homologue, overview Azotobacter vinelandii

Cofactor

Cofactor Comment Organism Structure
iron-molybdenum cofactor molybdenum-iron protein component with an iron-molybdenum cofactor center, biosynthesis of the cofactor, detailed overview. NifS and NifU launch the process by synthesizing small Fe/S fragments, such as the [Fe2S2] clusters and the [Fe4S4] clusters. These small Fe/S building blocks are assembled into a large Fe/S core on NifB and further processed on NifEN with the assistance of Fe protein. Upon the completion of assembly on NifEN, the mature FeMoco is subsequently delivered to its target location within theMoFe protein, resulting in the formation of an active holo-MoFe protein Azotobacter vinelandii
MgATP2- required Azotobacter vinelandii
additional information NifEN is a partially defective homologue of the MoFe protein, catalytic properties, overview. Components of the electron transfer chains in nitrogenase and its homologue, overview Azotobacter vinelandii

General Information

General Information Comment Organism
evolution NifEN and MoFe protein have evolved from the replication and divergence of a common ancestral gene. NifEN is catalytically active early on in the course of evolution, when the mantle of earth is likely more reduced. Later, NifEN might have gradually evolved into an effective enzyme with a wide range of substrates, i.e. the MoFe protein, while in the meantime adjusting its own role toward synthesizing a catalytically more powerful cofactor, i.e. the iron-molybdenum cofactor Azotobacter vinelandii
additional information primary sequences of NifEN and MoFe proteins Azotobacter vinelandii