1.18.6.1: nitrogenase
This is an abbreviated version!
For detailed information about nitrogenase, go to the full flat file.
Word Map on EC 1.18.6.1
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1.18.6.1
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nodule
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azotobacter
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nitrogen-fixing
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vinelandii
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diazotrophic
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acetylene
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symbiotic
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klebsiella
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ammonia
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pneumoniae
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cyanobacterium
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rhizobium
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anabaena
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heterocysts
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nitrate
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legume
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n2-fixing
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bacteroid
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hydrogenase
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epr
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free-living
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atmospheric
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nh3
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rubrum
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bradyrhizobium
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azospirillum
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rhodospirillum
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japonicum
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rhodobacter
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meliloti
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rhizosphere
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nostoc
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capsulatus
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pasteurianum
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brasilense
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microaerobic
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rhodopseudomonas
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leguminosarum
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leghemoglobin
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variabilis
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mgadp
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carbide
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dithionite-reduced
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endor
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biofertilizer
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flavodoxins
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drag
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symbioses
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bacteriochlorophyll
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synthesis
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agriculture
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energy production
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anoxygenic
- 1.18.6.1
- nodule
- azotobacter
-
nitrogen-fixing
- vinelandii
-
diazotrophic
- acetylene
-
symbiotic
- klebsiella
- ammonia
- pneumoniae
- cyanobacterium
- rhizobium
- anabaena
- heterocysts
- nitrate
-
legume
-
n2-fixing
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bacteroid
- hydrogenase
- epr
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free-living
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atmospheric
- nh3
- rubrum
- bradyrhizobium
- azospirillum
- rhodospirillum
- japonicum
- rhodobacter
- meliloti
-
rhizosphere
- nostoc
- capsulatus
- pasteurianum
- brasilense
-
microaerobic
- rhodopseudomonas
- leguminosarum
- leghemoglobin
- variabilis
- mgadp
-
carbide
-
dithionite-reduced
-
endor
-
biofertilizer
- flavodoxins
-
drag
-
symbioses
- bacteriochlorophyll
- synthesis
- agriculture
- energy production
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anoxygenic
Reaction
4 reduced ferredoxin
+
8 H+
+
Synonyms
ARA, dinitrogenase, EC 1.18.2.1, Kp2, Mo nitrogenase, Mo-dependent nitrogenase, Mo-Fe nitrogenase, Mo-nitrogenase, MoFe protein, MoFe-protein, molybdenum nitrogenase, molybdenum-containing nitrogenase, molybdenum-iron protein, molybdenum-nitrogenase, More, N2ase, nif, nif1, nif2, nifD, NifDK, NifH, NifH2, nifHDK, nifK, nifM, nitrogenase Fe protein, nitrogenase Fe-protein, nitrogenase FeVco, nitrogenase iron-protein, nitrogenase MoFe protein, nitrogenase MoFe-protein, nitrogenase molybdenum iron protein, nitrogenase molybdenum-iron protein, V-nitrogenase, vanadium nitrogenase, vanadium-nitrogenase, VnfDGK, VnfH
ECTree
1.18.6.1 nitrogenaseAdvanced search results
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results (Cofactor
Cofactor on EC 1.18.6.1 - nitrogenase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
iron cofactor
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the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein
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[4Fe-4S]-center
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NifB and NifEN are two essential elements immediately adjacent to each other along the biosynthetic pathway of FeMoco. The 8Fe-precursor is present in the NifEN entity of a synthetic NifEN-B fusion protein, and additional [Fe4S4]-type cluster species are present in the NifB entity of NifEN-B. The cluster species in NifEN-B consist of both SAM-motif- and non-SAM-motif-bound [Fe4S4]-type clusters. The non-SAM-motif [Fe4S4]-cluster is a NifB-bound intermediate of FeMoco assembly, which could be converted to the 8Fe-precursor in a SAM-dependent mechanism
ATP
2 MgATP binding sites on the iron protein, binding changes the redox status of the [4Fe4S] cluster of the iron protein, mechanism, overview
ATP
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the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein
FeMo cofactor
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structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein
FeMo cofactor
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bound at the active site, the MoFe protein, encoded by nifD and nifK. It is an alpha2beta2 heterotetramer with each nifD-encoded alpha subunit coordinating the FeMo cofactor that binds and reduces substrate, while alpha plus the nifK-encoded beta subunits coordinate the [8Fe-7S] P-cluster
FeMo cofactor
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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
FeMo cofactor
active site located, ability of the multimetallic catalytic FeMo cofactor cluster to accumulate multiple [e-/H+]
FeMo protein
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a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein, Fe6 within FeMo-cofactor provides the unique site for alkyne substrate binding and has van der Waals contact with the side chains of alpha-Val70l and alpha-Gln191, overview
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FeMo protein
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FeMo-co is composed of 7Fe, 9S, Mo, R-homocitrate, and one unidentified light atom, in vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified Nif proteins, Several nif genes are essential for FeMo-co synthesis in vivo, e.g., nifB, nifU, nifS, nifH, nifN, nifE, and nifV, modeling, overview
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iron-molybdenum cofactor
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dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the cofactor is composed of a [Mo-3Fe-3S] subcluster and a [4Fe3S] subcluster bridged by 3 sulfide pairs, with homocitrate bound to the molybdenum, structure determination and analysis
iron-molybdenum cofactor
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enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, structure, redox status, part of the MoFe protein
iron-molybdenum cofactor
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required for activity of the enzyme complex, insertion in the presynthesized apodinitrogenase involving the monomeric 26 kDa NafY protein, which binds the FeMo cofactor with very high affinity via its HIs121, the cofactor-NafY-complex exhibits an EPR signal similar to isolated FeMo cofactor and the M-center of the enzyme, NafY also binds the biosynthetic precursor of the MoFe cofactor, the NifB-cofacor, determination of binding sites
iron-molybdenum cofactor
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substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis
iron-molybdenum cofactor
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located at the active site in the MoFe protein
iron-molybdenum cofactor
modelling of the FeMo-cofactor binding site in the alpha70Ile MoFe protein structure
iron-molybdenum cofactor
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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
iron-molybdenum cofactor
the enzyme contains 2 [8Fe-7S] P clusters and 2 active site [7Fe-9S-C-Mo-homocitrate] iron-molybdenum cofactors
additional information
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structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer
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additional information
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structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer
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additional information
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structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer
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additional information
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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
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additional information
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the cofactors of the Mo- and V-nitrogenases, i.e. FeMoco and FeVco, are homologous metalccenters with distinct catalytic properties, differences in electronic properties and structural topology, overview
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