Information on EC 1.18.6.1 - nitrogenase:

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea


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EC NUMBERCOMMENTARY
1.18.6.1-

RECOMMENDED NAMEGeneOntology No.
nitrogenaseGO:0018697

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
----
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAnabaena sp., Azospirillum sp., Azotobacter sp., Chlorobium sp., Chromatium sp., Desulfovibrio sp., Frankia sp., Gloeothece sp., Rhizobium leguminosarum, Rhodobacter sphaeroides, Rhodopseudomonas sp.-440134
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme complex dissociation and association kinetics; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; Fe protein and MoFe protein are assumed to associate and dissociate to transfer a single electron to the substrates; mechanism, Fe protein cycleAzotobacter vinelandii-440138
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhodobacter capsulatus-440142
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAllochromatium vinosum-440142, 440144
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAnabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens, Rhizobium lupini-440144
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhodospirillum rubrum-440142, 440144
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAllochromatium vinosum-440143, 440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinCorynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp.-440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinLeptolyngbya boryana-440134, 440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinOrnithopus sativus-440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzotobacter chroococcum-440144, 440146
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzotobacter vinelandii, Clostridium pasteurianum-440142, 440144, 440146, 440147
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinPaenibacillus polymyxa-440144, 440146, 440147
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinCyanobacterium sp.-440148
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinKlebsiella pneumoniae-440142, 440144, 440146, 440147, 440149
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism; structure of V-containing enzyme formAzotobacter vinelandii-440150
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinBradyrhizobium japonicum-440143, 440145, 440151
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAnabaena variabilis-440148, 440152
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinKlebsiella pneumoniae-440134, 440140, 440143, 440145, 440152, 440157
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinBeggiatoa alba-440160
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzospirillum amazonense-440161
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhizobium sp.-440134, 440145, 440162
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhizobium lupini-440143, 440145, 440165
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanismAnabaena sp., Anabaena variabilis, Azospirillum brasilense-440166
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanismAzotobacter chroococcum-440150, 440166
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanismAzotobacter sp., Azotobacter vinelandii, Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Oscillatoria sp., Rhizobium sp.-440166
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhodospirillum rubrum-440134, 440143, 440145, 440166
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinXanthobacter autotrophicus-440168
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinPaenibacillus polymyxa-440134, 440143, 440145, 440169
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAnabaena cylindrica-440134, 440145, 440170
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhodobacter capsulatus-440171
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanismAzotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.-440174
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; MgATP/MgADP-dependent electron and proton transfer kineticsAzotobacter vinelandii-440175
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
iron-only enzyme is composed of 2 components: FeFe protein and Fe proteinRhodobacter capsulatus-440176
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; iron-only enzyme is composed of 2 components: FeFe protein and Fe proteinRhodobacter capsulatus-440177
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic electron flow from Fe protein to substrate via MoFe protein and MoFe protein-cofactorAzotobacter vinelandii-440179
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
C2H2 inhibition mechanism, structure model; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzotobacter vinelandii-440183
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzotobacter chroococcum-440143, 440145, 440167, 440186
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinClostridium pasteurianum-440134, 440143, 440145, 440153, 440159, 440164, 440180, 440186
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
structure of V-containing enzyme formAzotobacter vinelandii-440188
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzotobacter vinelandii-440134, 440143, 440145, 440153, 440154, 440155, 440156, 440158, 440163, 440178, 440180, 440181, 440182, 440184, 440186, 440187, 440189
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195Azotobacter vinelandii-658010
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
theoretical mechanisms of substrate binding to molybdenum or iron in the FeMo cofactor, modelingAzotobacter vinelandii-658040
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
overall catalytic mechanism, overview, structures of active site metal clusters, interactions of substrate and active site, active site relevant residues are Arg96, Val70, Gly69, and His195, substrate binding mechanism of complex components, mechanism of MgATP hydrolysis and electron transfer, overviewAzotobacter vinelandiiP00459658483
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
the active site is located on the MoFe protein, active site structure and substrate binding mechanismKlebsiella pneumoniae-658901
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
active site locationAzotobacter vinelandii-659426
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
first introduction of H at the NFe7MoS9(homocitrate) active site is via a water chain terminating at water 679 to S3B of the my3-S atoms of the active site. Discussion of subsequent movement of the H atoms around the NFe7MoS9(homocitrate) preparatory to the binding and hydrogenation of N2 and other substrates. S2B has a modulatory function and is not an H-entry siteAzotobacter vinelandii-674147
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
SEPR1 intermediate formed during turnover of the nitrogenase alpha-195Gln MoFe protein with C2H2 in H2O buffers, is a product complex with C2H4 bound as a ferracycle to a single Fe of the FeMo-cofactor active site. CO bridges two Fe of lo-Co, while the C2H4 of SEPR1 binds to one of these. Correlation with Lowe-Thorneley En kinetic stateAzotobacter vinelandii-674154
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
theoretical investigation of the binding of N2 to the Fe7MoS9N(homocitrate)(cysteine)(histidine) active site, calculation of reaction profiles and activation energies for the association and dissociation of N2. An endo-ny1-N2 coordination at Fe6 is most probableAzotobacter vinelandii-674202
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
reaction mechanism, overviewMethanococcus maripaludis-684881
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
reaction mechanism, determination of reaction intermediates, two-step relaxation of the nitrogenase H+/H+ intermediate during step-annealing,both steps show large solvent kinetic isotope effects, step A is the catalytically central state that is activated for N2 binding by the accumulation of 4 electrons, and step B accumulates 2 electrons, overviewAzotobacter vinelandii-689764
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzospirillum amazonense Y1--
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195Azotobacter vinelandii DJ1310--
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinAzotobacter vinelandii OP, Beggiatoa alba B18LD, Corynebacterium flavescens 301, Escherichia coli C-M 74--
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
the active site is located on the MoFe protein, active site structure and substrate binding mechanismKlebsiella pneumoniae M5a1--
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe proteinRhizobium sp. ORS571--
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; iron-only enzyme is composed of 2 components: FeFe protein and Fe protein; iron-only enzyme is composed of 2 components: FeFe protein and Fe proteinRhodobacter capsulatus B10S--

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
Chloroalkane and chloroalkene degradation00625 -
Metabolic pathways01100 -
Microbial metabolism in diverse environments01120 -
nitrogen fixation-N2FIX-PWY
Nitrogen metabolism00910 -

SYSTEMATIC NAMEIUBMB Comments
reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing)Requires Mg2+. It is composed of two proteins that can be separated but are both required for nitrogenase activity. Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron. The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin). Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia. The molybdenum may be replaced by vanadium or iron. The reduction is initiated by formation of hydrogen in stoichiometric amounts [2]. Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1 nitrogenase (flavodoxin)].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
ARALotus japonicus--699812
dinitrogenaseRhodobacter capsulatus--657985
EC 1.18.2.1--formerly-
Kp2Klebsiella pneumoniae--687822, 687823
Mo-nitrogenaseAzotobacter chroococcum--715261
Mo-nitrogenaseAzotobacter chroococcum YM68A---
molybdenum nitrogenaseKlebsiella pneumoniae--715017
molybdenum nitrogenaseKlebsiella pneumoniae UN1217---
molybdenum-containing nitrogenaseAnabaena sp.--713837
molybdenum-containing nitrogenaseAnabaena sp. PCC 7120---
molybdenum-nitrogenaseAzotobacter chroococcum--715261
NifDKKlebsiella pneumoniae--715017
NifDKKlebsiella pneumoniae UN1217---
NifH2Methanocaldococcus jannaschii--713656
nitrogenase Fe proteinKlebsiella pneumoniae--687822
nitrogenase Fe-proteinKlebsiella pneumoniae--687823
nitrogenase FeVcoAzotobacter chroococcum--715261
nitrogenase FeVcoAzotobacter chroococcum YM68A---
nitrogenase iron-proteinKlebsiella pneumoniae--687823
V-nitrogenaseAzotobacter chroococcum--715261
V-nitrogenaseAzotobacter chroococcum YM68A---
vanadium nitrogenaseAzotobacter vinelandii--716922
vanadium-nitrogenaseAzotobacter chroococcum--715261
vanadium-nitrogenaseAzotobacter chroococcum YM68A---
molybdenum-nitrogenaseAzotobacter chroococcum YM68A---
additional informationAzotobacter vinelandii-the nitrogenase complex is composed of 2 oxygen-labile metalloproteins: dinitrogenase and dinitrogenase reductase659338
additional informationAzotobacter vinelandii DJ-the nitrogenase complex is composed of 2 oxygen-labile metalloproteins: dinitrogenase and dinitrogenase reductase-

CAS REGISTRY NUMBERCOMMENTARY
9013-04-1-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Allochromatium vinosum-440142, 440143, 440144, 440145--Manually annotated by BRENDA team
Alnus maritimaenzyme activity increases with increasing concentration of O2 in the root zone. Photosynthetic rate, plant dry mass, leaf N content, and nodule fresh mass are maximal in plants maintained with 15-25% O2 in the root zone676442--Manually annotated by BRENDA team
Anabaena cylindrica-440134, 440144, 440145, 440170--Manually annotated by BRENDA team
Anabaena sp.-440134, 440166, 713837--Manually annotated by BRENDA team
Anabaena sp. PCC 7120-713837--Manually annotated by BRENDA team
Anabaena variabilis-440148, 440166--Manually annotated by BRENDA team
Anabaena variabilisnitrogen fixation complex is encoded on nif gene cluster440152--Manually annotated by BRENDA team
Azoarcus sp.strain BH72698619--Manually annotated by BRENDA team
Azoarcus sp. BH72strain BH72698619--Manually annotated by BRENDA team
Azospirillum amazonensestrain Y1440161--Manually annotated by BRENDA team
Azospirillum amazonense Y1strain Y1440161--Manually annotated by BRENDA team
Azospirillum brasilense-440166, 673723--Manually annotated by BRENDA team
Azospirillum sp.-440134--Manually annotated by BRENDA team
Azotobacter chroococcum-440143, 440144, 440145, 440146, 440150, 440166, 440167--Manually annotated by BRENDA team
Azotobacter chroococcumcontains Mo- and V-nitrogenases715261--Manually annotated by BRENDA team
Azotobacter chroococcumnitrogen fixation complex is encoded on nif gene cluster440186--Manually annotated by BRENDA team
Azotobacter chroococcum YM68Acontains Mo- and V-nitrogenases715261--Manually annotated by BRENDA team
Azotobacter sp.-440134, 440166--Manually annotated by BRENDA team
Azotobacter vinelandii-440134, 440138, 440142, 440143, 440144, 440145, 440146, 440147, 440153, 440154, 440156, 440158, 440163, 440166, 440174, 440175, 440178, 440181, 440183, 440184, 440187, 440189, 659426, 672039, 673039, 674147, 674154, 676778, 714796, 715263, 716924--Manually annotated by BRENDA team
Azotobacter vinelandii-658483P00459UniprotManually annotated by BRENDA team
Azotobacter vinelandii-715813P07328UniProtManually annotated by BRENDA team
Azotobacter vinelandii2 forms of VFe protein440188--Manually annotated by BRENDA team
Azotobacter vinelandii2 forms of VFe protein; nitrogen fixation complex is encoded on nif gene cluster440186--Manually annotated by BRENDA team
Azotobacter vinelandii; recombinant strain DJ1373 expressing mutant V70I689764--Manually annotated by BRENDA team
Azotobacter vinelandiicontains 3 classes of nitrogenase, the second contains V, the third is encoded by a separate set of genes and is lacking V and Mo and is inhibited by V and Mo440150, 440155--Manually annotated by BRENDA team
Azotobacter vinelandiicontains nif-encoded molybdenum nitrogenase and vnf-encoded V nitrogenase716922--Manually annotated by BRENDA team
Azotobacter vinelandiimolybdenum-dependent enzyme variant658040--Manually annotated by BRENDA team
Azotobacter vinelandiinitrogen fixation complex is encoded on nif gene cluster440179, 440182--Manually annotated by BRENDA team
Azotobacter vinelandiistrain DJ659338--Manually annotated by BRENDA team
Azotobacter vinelandiistrain DJ1310658010--Manually annotated by BRENDA team
Azotobacter vinelandiistrain DJ995688191--Manually annotated by BRENDA team
Azotobacter vinelandiistrain OP440180--Manually annotated by BRENDA team
Azotobacter vinelandiitheoretical investigation of the binding of N2 to the Fe7MoS9N(homocitrate)(cysteine)(histidine) active site, calculation of reaction profiles and activation energies for the association and dissociation of N2674202--Manually annotated by BRENDA team
Azotobacter vinelandii DJstrain DJ659338--Manually annotated by BRENDA team
Azotobacter vinelandii DJ1310strain DJ1310658010--Manually annotated by BRENDA team
Azotobacter vinelandii DJ995strain DJ995688191--Manually annotated by BRENDA team
Azotobacter vinelandii OPstrain OP440180--Manually annotated by BRENDA team
Beggiatoa albastrain B18LD440160--Manually annotated by BRENDA team
Beggiatoa alba B18LDstrain B18LD440160--Manually annotated by BRENDA team
Bradyrhizobium japonicum-440143, 440144--Manually annotated by BRENDA team
Bradyrhizobium japonicumassociated with Glycine max440145--Manually annotated by BRENDA team
Bradyrhizobium japonicumnitrogen fixation complex is encoded on nif gene cluster440151--Manually annotated by BRENDA team
Bradyrhizobium japonicumstrains 110 or 2134, anaerobically and aerobically isolated bacteroid from nodules of soybean660287--Manually annotated by BRENDA team
Chlorobium sp.-440134--Manually annotated by BRENDA team
Chromatium sp.-440134, 440174--Manually annotated by BRENDA team
Clostridium pasteurianum-440134, 440142, 440143, 440144, 440145, 440146, 440147, 440153, 440159, 440164, 440174, 440180--Manually annotated by BRENDA team
Clostridium pasteurianumnitrogen fixation complex is encoded on nif gene cluster440186--Manually annotated by BRENDA team
Corynebacterium flavescens-440144--Manually annotated by BRENDA team
Corynebacterium flavescens301440145--Manually annotated by BRENDA team
Corynebacterium flavescens 301301440145--Manually annotated by BRENDA team
Crocosphaera watsoniia marine unicellular diazotrophic cyanobacterium714845--Manually annotated by BRENDA team
Crocosphaera watsonii WH8501a marine unicellular diazotrophic cyanobacterium714845--Manually annotated by BRENDA team
Cyanobacterium sp.-440148--Manually annotated by BRENDA team
Desulfovibrio desulfuricanslow activity440145--Manually annotated by BRENDA team
Desulfovibrio sp.-440134--Manually annotated by BRENDA team
Escherichia coliC-M 74440145--Manually annotated by BRENDA team
Escherichia coli C-M 74C-M 74440145--Manually annotated by BRENDA team
Frankia sp.-440134, 440166--Manually annotated by BRENDA team
Gloeocapsa sp.-440145--Manually annotated by BRENDA team
Gloeothece sp.-440134, 440166--Manually annotated by BRENDA team
Gloeothece sp.a terrestrial unicellular diazotrophic cyanobacterium714845--Manually annotated by BRENDA team
Gloeothece sp. PCC6909a terrestrial unicellular diazotrophic cyanobacterium714845--Manually annotated by BRENDA team
Gluconacetobacter diazotrophicusexpression of nitrogenase in the absence of NH4+ and at initial O2 concentrations above 5% in the culture atmosphere672344--Manually annotated by BRENDA team
Gluconacetobacter diazotrophicusstrain PAL-5, in endosymbiosis with sugarcane, Saccharum officinarum658372--Manually annotated by BRENDA team
Gluconacetobacter diazotrophicus PAL-5strain PAL-5, in endosymbiosis with sugarcane, Saccharum officinarum658372--Manually annotated by BRENDA team
Herbaspirillum seropedicae-658769--Manually annotated by BRENDA team
Klebsiella pneumoniae-440134, 440140, 440142, 440143, 440144, 440145, 440146, 440149, 440157, 440166, 440174, 687822, 687823, 715017--Manually annotated by BRENDA team
Klebsiella pneumoniaenitrogen fixation complex is encoded on nif gene cluster440147, 440152--Manually annotated by BRENDA team
Klebsiella pneumoniaestrain M5a1658901--Manually annotated by BRENDA team
Klebsiella pneumoniae M5a1strain M5a1658901--Manually annotated by BRENDA team
Klebsiella pneumoniae UN1217-715017--Manually annotated by BRENDA team
Leptolyngbya boryana-440134, 440145--Manually annotated by BRENDA team
Lotus japonicusinoculated with symbiont Mesorhizobium loti strain New Zealand Palmerston 2235699812--Manually annotated by BRENDA team
Mesorhizobium loti-716483--Manually annotated by BRENDA team
Methanocaldococcus jannaschiiNifH2 is one of two homologues of NifH in Methanocaldococcus jannaschii713656--Manually annotated by BRENDA team
Methanococcus maripaludis-676049, 684881--Manually annotated by BRENDA team
Ornithopus sativus-440145--Manually annotated by BRENDA team
Oscillatoria sp.-440166--Manually annotated by BRENDA team
Paenibacillus polymyxa-440134, 440143, 440144, 440145, 440146, 440147, 440169--Manually annotated by BRENDA team
Rhizobium leguminosarum-440134--Manually annotated by BRENDA team
Rhizobium lupini-440143, 440144, 440165--Manually annotated by BRENDA team
Rhizobium lupiniassociated with Lupinus luteus440145--Manually annotated by BRENDA team
Rhizobium sp.-440166, 440174--Manually annotated by BRENDA team
Rhizobium sp.associated with Phaseolus aureus or Vigna sinensis440145--Manually annotated by BRENDA team
Rhizobium sp.ORS571440134--Manually annotated by BRENDA team
Rhizobium sp.ORS571, associated with Sesbania rostrata440162--Manually annotated by BRENDA team
Rhizobium sp. ORS571ORS571440134--Manually annotated by BRENDA team
Rhodobacter capsulatus-440142, 440171--Manually annotated by BRENDA team
Rhodobacter capsulatusiron-only nitrogenase and molybdenum nitrogenase; nitrogen fixation complex is encoded on nif gene cluster; strain B10S440176, 440177--Manually annotated by BRENDA team
Rhodobacter capsulatuswild-type strain B10S, molybdenum-containing, nif-encoded enzyme variant657985--Manually annotated by BRENDA team
Rhodobacter capsulatus B10Sstrain B10S440176, 440177--Manually annotated by BRENDA team
Rhodobacter sphaeroides-440134--Manually annotated by BRENDA team
Rhodopseudomonas sp.-440134--Manually annotated by BRENDA team
Rhodospirillum rubrum-440134, 440142, 440143, 440144, 440145, 440166, 662028--Manually annotated by BRENDA team
Xanthobacter autotrophicus-440168--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
evolutionAzotobacter vinelandii-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 cofactor714796
evolutionKlebsiella pneumoniae-substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview715017
evolutionAzotobacter vinelandii-the ability of V nitrogenase to catalyze both CO and N2 reductions suggests a potential link between the evolution of carbon and nitrogen cycles716922
physiological functionAnabaena sp.-nitrogenase, an oxygen-labile enzyme typically containing an iron-molybdenum cofactor active site, is responsible for nitrogen fixation producing photobiological H2 as a byproduct713837
physiological functionKlebsiella pneumoniae-the conversion of N2 into NH3 is catalyzed by the nitrogenase enzyme, which is composed of two metalloproteins: NifDK, also termed dinitrogenase or MoFe protein, and NifH, also termed dinitrogenase reductase or Fe protein715017
physiological functionAzotobacter vinelandii-the diminished H2 evolution by V nitrogenase originates from the diversion of electrons toward CO reduction, in contrast to the Mo nitrogenase716922
physiological functionAnabaena sp. PCC 7120-nitrogenase, an oxygen-labile enzyme typically containing an iron-molybdenum cofactor active site, is responsible for nitrogen fixation producing photobiological H2 as a byproduct-
physiological functionKlebsiella pneumoniae UN1217-the conversion of N2 into NH3 is catalyzed by the nitrogenase enzyme, which is composed of two metalloproteins: NifDK, also termed dinitrogenase or MoFe protein, and NifH, also termed dinitrogenase reductase or Fe protein-
evolutionKlebsiella pneumoniae UN1217-substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview-
additional informationMethanocaldococcus jannaschii-nitrogenase is a protein complex that is required for biological nitrogen fixation. It is made up of a nitrogenase, which is a NifD2/NifK2 heterotetramer, and a nitrogenase reductase, which is a homodimer of NifH713656
additional informationAnabaena sp.-nitrogenase consists of the Fe protein, encoded by nifH, and the MoFe protein, encoded by nifD and nifK. The Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein, which is bound at the active site and 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-cluster713837
additional informationAzotobacter vinelandii-primary sequences of NifEN and MoFe proteins714796
additional informationCrocosphaera watsonii, Gloeothece sp.-pattern of nitrogenase activity during the light-dark cycle, overview714845
additional informationAzotobacter vinelandiiP07328structure of the alpha70Ile MoFe protein compared to the alpha70Val wild-type MoFe protein, shows a delta-methyl group of alpha70Val that is positioned over Fe6 within the active site FeMo-cofactor715813
additional informationAzotobacter vinelandii-like the nif-encoded molybdenum nitrogenase, the vnf-encoded V nitrogenase is composed of a specific reductant and a catalytic component. Both nitrogenases use a catalytic mechanism that involves ATP-dependent electron transfer from a reductant, the nifH- or vnfH-encoded Fe protein, to the catalytic component, i.e. nifDK-encoded MoFe protein or vnfDGK-encoded VFe protein, and the reduction of N2 at the cofactor site, i.e. FeMoco or FeVco, of the latter716922
additional informationAzotobacter vinelandii-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, overview716924
additional informationAnabaena sp. PCC 7120-nitrogenase consists of the Fe protein, encoded by nifH, and the MoFe protein, encoded by nifD and nifK. The Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein, which is bound at the active site and 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-
additional informationCrocosphaera watsonii WH8501, Gloeothece sp. PCC6909-pattern of nitrogenase activity during the light-dark cycle, overview-

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(VO4)3- + ?(VO2)+ + ?
show the reaction diagram
Azotobacter vinelandii-reduction of vanadium(V) by reduced Fe-protein of enzyme to vanadium(IV), which then probably binds to the nucleotide binding site in place of the Mg2+ which is normally present. The oxidized Fe-protein is unable to reduce vanadate673039--?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Escherichia coli, Bradyrhizobium japonicum--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus--440142-440142?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus--440176-440176?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus--440177-440177?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Klebsiella pneumoniae--440142-440142?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Klebsiella pneumoniae--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Klebsiella pneumoniae--440146-440146?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Klebsiella pneumoniae--440157-440157?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Klebsiella pneumoniae--440174-440174?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Clostridium pasteurianum--440142-440142?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Clostridium pasteurianum--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Clostridium pasteurianum--440146-440146?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Clostridium pasteurianum--440174-440174?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Clostridium pasteurianum--440186-440186?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440142-440142?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440146-440146?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440154-440154?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440158-440158?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440174-440174?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440178-440178?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440181-440181?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440182-440182?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440183-440183?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440186-440186?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440187-440187?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440188-440188?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Paenibacillus polymyxa--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Paenibacillus polymyxa--440146-440146?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Paenibacillus polymyxa--440169-440169?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodospirillum rubrum--440142-440142?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodospirillum rubrum--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Chromatium sp.--440174-440174?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhizobium sp.--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhizobium sp.--440174-440174?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Desulfovibrio desulfuricans--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Allochromatium vinosum--440142-440142?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Allochromatium vinosum, Rhizobium lupini, Anabaena cylindrica--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Anabaena cylindrica--440170-440170?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter chroococcum--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter chroococcum--440146-440146?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter chroococcum--440186-440186?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Leptolyngbya boryana--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Xanthobacter autotrophicus--440168-440168?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Gloeocapsa sp., Corynebacterium flavescens, Ornithopus sativus--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Cyanobacterium sp.--440148-440148?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii-active site for acetylene reduction interacts not directly with N2 reduction440183---
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii-anaerobic atmosphere440189reduction cycle continues until complete reduction of the substrate to ethane440189?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azoarcus sp., Azoarcus sp. BH72-ferredoxin is the main but not the essential electron donor for nitrogenase698619--?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Corynebacterium flavescens 301--440145-440145?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S--440176-440176?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S--440177-440177?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Escherichia coli C-M 74--440145-440145?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
Rhodobacter capsulatus, Klebsiella pneumoniae, Clostridium pasteurianum, Azotobacter vinelandii--440142--?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
Azotobacter vinelandii--440150--?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
Rhodospirillum rubrum, Allochromatium vinosum--440142--?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
Azotobacter vinelandii-intermediate is a flavodoxin hydroquinone440138-440138?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Escherichia coli--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter sphaeroides--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Bradyrhizobium japonicum--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Bradyrhizobium japonicum--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Bradyrhizobium japonicum--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Bradyrhizobium japonicum--440151-440151?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus--440142-440142?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus--440171-440171?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus--440176-440176?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus--440177-440177?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440140-440140?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440142-440142?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440146-440146?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440147-440147?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440149-440149?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440152-440152?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440157-440157?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440142-440142?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440146-440146?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440147-440147?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440153-440153?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440159-440159?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440164-440164?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440180-440180?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440138, 440142--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440142-440142?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440146-440146?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440147-440147?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440150-440150?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440153-440153?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440154, 440155--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440155-440155?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440156-440156?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440158-440158?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440163-440163?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440175, 440178--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440178-440178?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440179-440179?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440180-440180?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440181-440181?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440182, 440183--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440183-440183?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440184-440184?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440187-440187?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440188-440188?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440189-440189?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440146-440146?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440147-440147?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440169-440169?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum brasilense--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440142-440142?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chromatium sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chromatium sp.--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp.--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp.--440162-440162?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp.--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp.--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium leguminosarum--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Desulfovibrio desulfuricans--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodopseudomonas sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Allochromatium vinosum--440142-440142?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Allochromatium vinosum--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Allochromatium vinosum--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Allochromatium vinosum--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena variabilis--440148-440148?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena variabilis--440152-440152?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena variabilis--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Desulfovibrio sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium lupini--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium lupini--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium lupini--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium lupini--440165-440165?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena sp.--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena cylindrica--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena cylindrica--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena cylindrica--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena cylindrica--440170-440170?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum amazonense--440161-440161?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Frankia sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Frankia sp.--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440143-440143?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440146-440146?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440150-440150?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440167-440167?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Leptolyngbya boryana--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Leptolyngbya boryana--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter sp.--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Xanthobacter autotrophicus--440168-440168?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeocapsa sp.--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chlorobium sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Oscillatoria sp.--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens--440144-440144?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Ornithopus sativus--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.--440148-440148?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Beggiatoa alba--440160-440160?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum sp., Gloeothece sp.--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeothece sp.--440166-440166?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-slow enzyme440138-440138?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-1-propyne, 1-butyne and allene are reduced to the corresponding alkenes440154-440154?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-Fe protein and MoFe protein are assumed to associate and dissociate to transfer a single electron to the substrates, termed Fe protein cycle, driven by MgATP hydrolysis, with the dissociation of the Fe protein-MoFe protein complex being the rate limiting step of the cycle440138-440138?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum-MgATP-dependent440186-440186?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-MgATP-dependent440175-440175?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-MgATP-dependent440182-440182?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii, Azotobacter chroococcum-MgATP-dependent440186-440186?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.-ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin, regulation440148--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter sphaeroides, Klebsiella pneumoniae, Clostridium pasteurianum-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum-biological N2 fixation440186--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-biological N2 fixation440134, 440186--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-biological N2 fixation440188-440188?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa, Rhodospirillum rubrum, Chromatium sp., Rhizobium sp., Rhizobium leguminosarum, Rhodopseudomonas sp., Desulfovibrio sp., Anabaena sp., Anabaena cylindrica, Frankia sp.-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum-biological N2 fixation440186--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Leptolyngbya boryana, Azotobacter sp., Chlorobium sp.-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.-biological N2 fixation440148--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeothece sp.-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter sphaeroides, Clostridium pasteurianum, Paenibacillus polymyxa, Rhodospirillum rubrum, Chromatium sp., Rhizobium sp., Rhizobium leguminosarum, Rhodopseudomonas sp., Desulfovibrio sp., Anabaena sp., Anabaena cylindrica, Frankia sp., Leptolyngbya boryana, Chlorobium sp., Gloeothece sp.-ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum amazonense Y1--440161-440161?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii OP--440180-440180?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp. ORS571--440134-440134?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp. ORS571-biological N2 fixation, ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens 301--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S--440176-440176?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S--440177-440177?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Escherichia coli C-M 74--440145-440145?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Beggiatoa alba B18LD--440160-440160?
acetylene + ?ethylene + ?
show the reaction diagram
Bradyrhizobium japonicum--660287--?
acetylene + ?ethylene + ?
show the reaction diagram
Rhodobacter capsulatus--657985--?
acetylene + ?ethylene + ?
show the reaction diagram
Klebsiella pneumoniae--658901--?
acetylene + ?ethylene + ?
show the reaction diagram
Azotobacter vinelandii--658040--?
acetylene + ?ethylene + ?
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
acetylene + ?ethylene + ?
show the reaction diagram
Azotobacter vinelandii--659426--?
acetylene + ?ethylene + ?
show the reaction diagram
Herbaspirillum seropedicae--658769--?
acetylene + ?ethylene + ?
show the reaction diagram
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL-5--658372--?
acetylene + ?ethylene + ?
show the reaction diagram
Klebsiella pneumoniae M5a1--658901--?
C2H2 + ??
show the reaction diagram
Azotobacter vinelandii, Azotobacter vinelandii DJ1310--658010--?
C2H2 + ?H2 + ?
show the reaction diagram
Gluconacetobacter diazotrophicus--672344--?
CS2 + ?H2S + ?
show the reaction diagram
Azotobacter vinelandiiP00459slow turnover658483--?
cyanamide + ??
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
cyanide + ??
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
cyanide + ??
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1-cyanide favors the molydenum for binding658901--?
cyclopropene + ??
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1--658901--?
dithionite + H+ + acetylene + ATP?
show the reaction diagram
Azospirillum amazonense, Azospirillum amazonense Y1--440161--?
dithionite + H+ + N2 + ATP?
show the reaction diagram
Klebsiella pneumoniae-in vitro substrate440140, 440157, 440174--?
dithionite + H+ + N2 + ATP?
show the reaction diagram
Clostridium pasteurianum-in vitro substrate440174, 440180--?
dithionite + H+ + N2 + ATP?
show the reaction diagram
Azotobacter vinelandii-in vitro substrate440138, 440150, 440156, 440174, 440175, 440180, 440187--?
dithionite + H+ + N2 + ATP?
show the reaction diagram
Anabaena cylindrica-in vitro substrate440170--?
dithionite + H+ + N2 + ATP?
show the reaction diagram
Azotobacter vinelandii-SO2- being the actual nitrogenase reductant, reaction kinetics440187--?
dithionite + H+ + N2 + ATP?
show the reaction diagram
Azotobacter vinelandii OP-in vitro substrate440180--?
ethylene + ??
show the reaction diagram
Rhodobacter capsulatus--657985--?
ethylene + ??
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1--658901--?
hydrazine + ??
show the reaction diagram
Azotobacter vinelandii-high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme659426--?
methyl isocyanide + ??
show the reaction diagram
Klebsiella pneumoniae--658901--?
N2 + 8 e- + 16 ATP + 8 H+2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3, relaxation of the nitrogenase H+/H+ intermediate during step-annealing689764--?
N2 + 8 e- + 8 H+ + 16 ATP2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview715263--ir
N2H4 + ??
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
N2O + ??
show the reaction diagram
Klebsiella pneumoniae--658901--?
N2O + ??
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
N3- + ??
show the reaction diagram
Klebsiella pneumoniae--658901--?
N3- + ??
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
propargyl alcohol + ??
show the reaction diagram
Azotobacter vinelandii, Azotobacter vinelandii DJ1310-wild-type enzyme and V70A mutant MoFe protein-containing enzyme658010--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440184-440184?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440187-440187?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440189-440189?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Escherichia coli, Bradyrhizobium japonicum, Klebsiella pneumoniae-in absence of other acceptors440145--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae-in absence of other acceptors440146--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum-in absence of other acceptors440145, 440146--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii-in absence of other acceptors440145, 440146, 440158--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Paenibacillus polymyxa-in absence of other acceptors440145, 440146--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Rhodospirillum rubrum, Rhizobium sp., Desulfovibrio desulfuricans, Allochromatium vinosum, Rhizobium lupini, Anabaena cylindrica, Azotobacter chroococcum-in absence of other acceptors440145--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Azotobacter chroococcum-in absence of other acceptors440146--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Leptolyngbya boryana, Gloeocapsa sp., Corynebacterium flavescens, Ornithopus sativus-in absence of other acceptors440145--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Rhodobacter capsulatus-H2-producing activity is much higher in the iron-only enzyme form than in the molybdenum containing form and is less inhibited by competitive substrates440176-440176?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Corynebacterium flavescens 301-in absence of other acceptors440145--?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Rhodobacter capsulatus B10S-H2-producing activity is much higher in the iron-only enzyme form than in the molybdenum containing form and is less inhibited by competitive substrates440176-440176?
reduced ferredoxin + H+ + ATPoxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Escherichia coli C-M 74-in absence of other acceptors440145--?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--440145-440145?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--440174--?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440145-440145?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440174--?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440145-440145?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440154-440154?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440158-440158?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440174--?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Paenibacillus polymyxa, Rhodospirillum rubrum--440145-440145?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Chromatium sp.--440174--?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Rhizobium sp.--440145, 440174--?
reduced ferredoxin + H+ + CH3NC + ATPoxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Azotobacter chroococcum--440145-440145?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--440146-440146?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--440174-440174?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440146-440146?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440174-440174?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440186-440186?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440146-440146?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440174-440174?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440178-440178?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440181-440181?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440186-440186?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Paenibacillus polymyxa--440146-440146?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Chromatium sp.--440174-440174?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Rhizobium sp.--440174-440174-
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter chroococcum--440146-440146?
reduced ferredoxin + H+ + CN- + ATPoxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter chroococcum--440186-440186?
reduced ferredoxin + H+ + N2 + ATPoxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--687822, 687823--?
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Bradyrhizobium japonicum--660287--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--658901--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--658010, 659426--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Herbaspirillum seropedicae--658769--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Methanococcus maripaludis--684881--?
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus--658372--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii-biological nitrogen fixation658040--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus-biological nitrogen fixation658372--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandiiP00459enzyme complex is responsible for the majority of biological nitrogen fixation658483--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Bradyrhizobium japonicum-reduction of atmospheric dinitrogen to ammonium660287--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii-in absence of N2 or other substrates, the electron flow is directed towards proton reduction658040--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandiiP00459turnover cycle scheme, MgATP is required for activity, mechanism of MgATP hydrolysis and electron transfer with an important role of switch I and II within the Fe protein658483--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus PAL-5-biological nitrogen fixation658372--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii DJ1310--658010--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae M5a1--658901--ir
reduced ferredoxin + H+ + N2O + ATPoxidized ferredoxin + H2O + N2 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae, Clostridium pasteurianum, Azotobacter vinelandii, Paenibacillus polymyxa, Azotobacter chroococcum--440146-440146?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--440146-440146?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--440174-440174?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440146-440146?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440174-440174?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Clostridium pasteurianum--440186-440186?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440146-440146?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440154-440154?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440158-440158?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440174-440174?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440178-440178?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440186-440186?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Paenibacillus polymyxa--440146-440146?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Chromatium sp., Rhizobium sp.--440174-440174?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter chroococcum--440146-440146?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter chroococcum--440186-440186?
reduced ferredoxin + H+ + N3- + ATPoxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii-mutant H195Q shows only about 7.5% activity compared to wild-type440184-440184?
reduced ferredoxin + H+ + SCN- + ATPoxidized ferredoxin + H2S + HCN + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--440178-440178?
Ti3+ + H+ + N2 + ATP?
show the reaction diagram
Clostridium pasteurianum, Azotobacter vinelandii, Azotobacter vinelandii OP-in vitro substrate440180--?
methyl isocyanide + ??
show the reaction diagram
Azotobacter vinelandiiP00459-658483--?
additional information?-Herbaspirillum seropedicae-gene nifX and the contigous gene orf1 are essential for maximum nitrogen fixation under iron limitation and are probably involved in synthesis of nitrogenase iron or iron-molybdenum clusters658769---
additional information?-Gluconacetobacter diazotrophicus-influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview658372---
additional information?-Azotobacter vinelandiiP00459the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview, catalytic role of the molybdenum-iron protein, with P-cluster, and the Fe protein658483---
additional information?-Methanococcus maripaludis-both nifI1 and nifI2 are required for regulation in vivo684881---
additional information?-Azotobacter vinelandii-nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth, substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview688191---
additional information?-Methanococcus maripaludis-the enzyme performs acetylene reduction684881---
additional information?-Mesorhizobium loti-enzyme activity causes acetylene production716483---
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 cofactor714796---
additional information?-Azotobacter chroococcum-FeVco is extracted intact, carrying with it the characteristic capacity to reduce C2H2 to C2H6 and, perhaps even more importantly, the ability to reduce N2 to NH3715261---
additional information?-Klebsiella pneumoniae-substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3715017---
additional information?-Azotobacter vinelandiiP07328substrates bind and are reduced at a single 4Fe-4S face of the FeMo-cofactor. When alpha70Val is substituted by alpha70Ile, access of substrates to Fe6 of this face is effectively blocked715813---
additional information?-Azotobacter vinelandii DJ995-nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth, substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview688191---
additional information?-Klebsiella pneumoniae UN1217-substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3715017---
additional information?-Gluconacetobacter diazotrophicus PAL-5-influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview658372---
additional information?-Azotobacter chroococcum YM68A-FeVco is extracted intact, carrying with it the characteristic capacity to reduce C2H2 to C2H6 and, perhaps even more importantly, the ability to reduce N2 to NH3715261---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Azotobacter vinelandii--440183-440183?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Anabaena cylindrica--440170--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Escherichia coli--440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Bradyrhizobium japonicum--440143, 440144, 440145, 440151--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus--440142, 440171, 440176, 440177--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440140, 440142, 440143, 440144, 440145, 440146, 440147, 440149, 440152, 440157, 440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Klebsiella pneumoniae--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum--440142, 440143, 440144, 440145, 440146, 440147, 440153, 440159, 440164, 440174, 440180--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440138, 440142, 440143, 440144, 440145, 440146, 440147, 440150, 440153, 440154, 440155, 440156, 440158, 440163, 440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440174-440174?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--440175, 440178, 440179, 440180, 440181, 440182, 440183, 440184, 440187--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa--440143, 440144, 440145, 440146, 440147, 440169--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum brasilense--440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodospirillum rubrum--440142, 440143, 440144, 440145, 440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chromatium sp.--440174--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp.--440145, 440162, 440166, 440174--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Desulfovibrio desulfuricans--440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Allochromatium vinosum--440142, 440143, 440144, 440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena variabilis--440148, 440152, 440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium lupini--440143, 440144, 440145, 440165--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena sp.--440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Anabaena cylindrica--440144, 440145, 440170--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum amazonense--440161--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Frankia sp.--440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum--440143, 440144, 440145, 440146, 440150, 440166, 440167--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Leptolyngbya boryana--440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter sp.--440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Xanthobacter autotrophicus--440168--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeocapsa sp.--440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Oscillatoria sp.--440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens--440144, 440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Ornithopus sativus--440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Beggiatoa alba--440160--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum sp.--440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeothece sp.--440166--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.-ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin, regulation440148--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter sphaeroides, Klebsiella pneumoniae, Clostridium pasteurianum-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Clostridium pasteurianum-biological N2 fixation440186--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-biological N2 fixation440134, 440186--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-biological N2 fixation440188-440188?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Paenibacillus polymyxa, Rhodospirillum rubrum, Chromatium sp., Rhizobium sp., Rhizobium leguminosarum, Rhodopseudomonas sp., Desulfovibrio sp., Anabaena sp., Anabaena cylindrica, Frankia sp.-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter chroococcum-biological N2 fixation440186--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Leptolyngbya boryana, Azotobacter sp., Chlorobium sp.-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.-biological N2 fixation440148--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeothece sp.-biological N2 fixation440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter sphaeroides, Clostridium pasteurianum, Paenibacillus polymyxa, Rhodospirillum rubrum, Chromatium sp., Rhizobium sp., Rhizobium leguminosarum, Rhodopseudomonas sp., Desulfovibrio sp., Anabaena sp., Anabaena cylindrica, Frankia sp., Leptolyngbya boryana, Chlorobium sp., Gloeothece sp.-ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum amazonense Y1--440161--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii OP--440180--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp. ORS571-biological N2 fixation, ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase440134--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens 301--440145--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S--440176, 440177--?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Escherichia coli C-M 74--440145--?
N2 + 8 e- + 16 ATP + 8 H+2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii-the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3689764--?
N2 + 8 e- + 8 H+ + 16 ATP2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii--715263--ir
reduced ferredoxin + H+ + N2 + ATPoxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--687822, 687823--?
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae--658901--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii--658010, 659426--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Herbaspirillum seropedicae--658769--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Methanococcus maripaludis--684881--?
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii-biological nitrogen fixation658040--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus-biological nitrogen fixation658372--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandiiP00459enzyme complex is responsible for the majority of biological nitrogen fixation658483--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Bradyrhizobium japonicum-reduction of atmospheric dinitrogen to ammonium660287--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus PAL-5-biological nitrogen fixation658372--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii DJ1310--658010--ir
reduced ferredoxin + H+ + N2 + ATP + H2Ooxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae M5a1--658901--ir
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Beggiatoa alba B18LD--440160--?
additional information?-Herbaspirillum seropedicae-gene nifX and the contigous gene orf1 are essential for maximum nitrogen fixation under iron limitation and are probably involved in synthesis of nitrogenase iron or iron-molybdenum clusters658769---
additional information?-Gluconacetobacter diazotrophicus-influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview658372---
additional information?-Azotobacter vinelandiiP00459the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview658483---
additional information?-Methanococcus maripaludis-both nifI1 and nifI2 are required for regulation in vivo684881---
additional information?-Azotobacter vinelandii-nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth688191---
additional information?-Mesorhizobium loti-enzyme activity causes acetylene production716483---
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 cofactor714796---
additional information?-Azotobacter vinelandii DJ995-nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth688191---
additional information?-Gluconacetobacter diazotrophicus PAL-5-influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview658372---

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPGluconacetobacter diazotrophicus--658372 2D-image
ATPAzotobacter vinelandiiP004592 MgATP binding sites on the iron protein, binding changes the redox status of the [4Fe4S] cluster of the iron protein, mechanism, overview658483 2D-image
ATPHerbaspirillum seropedicae--658769 2D-image
ATPBradyrhizobium japonicum--660287 2D-image
ATPMethanococcus maripaludis--684881 2D-image
ATPKlebsiella pneumoniae-the FeS cluster exhibits very little change upon MgATP binding687822 2D-image
ATPAzoarcus sp.--698619 2D-image
ATPAnabaena sp.-the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein713837 2D-image
ATPKlebsiella pneumoniae--658901, 687823, 715017 2D-image
ATPAzotobacter vinelandii--658040, 688191, 689764, 715263, 716922 2D-image
FeMo cofactorMethanococcus maripaludis--684881-
FeMo cofactorAzotobacter vinelandii-structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein688191-
FeMo cofactorAnabaena sp.-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-cluster713837-
FeMo cofactorAzotobacter chroococcum-i.e. FeMoco cofactor, in the Mo-nitrogenase715261-
FeMo cofactorAzotobacter vinelandii-binding structure and mechanism, overview715263-
FeMo cofactorAzotobacter vinelandii-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, overview716924-
FeMo proteinAzotobacter vinelandii-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, overview688191-
FeMo proteinAzotobacter vinelandii-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, overview689764-
FerredoxinGluconacetobacter diazotrophicus--658372-
FerredoxinHerbaspirillum seropedicae--658769-
FerredoxinKlebsiella pneumoniae--658901-
FerredoxinAzotobacter vinelandii--658010, 658040, 658483, 659426-
FerredoxinBradyrhizobium japonicum--660287-
iron cofactorAnabaena sp.-the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein713837-
iron-molybdenum cofactorRhodobacter capsulatus--657985 2D-image
iron-molybdenum cofactorAzotobacter vinelandii-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 analysis658010 2D-image
iron-molybdenum cofactorAzotobacter vinelandii-enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, structure, redox status, part of the MoFe protein658040 2D-image
iron-molybdenum cofactorKlebsiella pneumoniae--658901 2D-image
iron-molybdenum cofactorAzotobacter vinelandii-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 sites659338 2D-image
iron-molybdenum cofactorAzotobacter vinelandii-substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis659426 2D-image
iron-molybdenum cofactorAzotobacter vinelandii-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 protein714796 2D-image
iron-molybdenum cofactorKlebsiella pneumoniae-located at the active site in the MoFe protein715017 2D-image
iron-molybdenum cofactorAzotobacter vinelandiiP07328modelling of the FeMo-cofactor binding site in the alpha70Ile MoFe protein structure715813 2D-image
iron-vanadium cofactorAzotobacter chroococcum-i.e. FeVco cofactor, in the V-nitrogenase715261-
MgATP2-Azotobacter vinelandii-required714796 2D-image
additional informationAzotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum-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 transfer440186-
additional informationAzotobacter vinelandii-structure of MoFe-cofactor440189-
additional informationAzotobacter vinelandii-NifEN is a partially defective homologue of the MoFe protein, catalytic properties, overview. Components of the electron transfer chains in nitrogenase and its homologue, overview714796-
additional informationAzotobacter chroococcum-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, overview715261-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ca2+Klebsiella pneumoniae-1.2 gatom per mol of MoFe protein440149
Co2+Azotobacter vinelandii-divalent cation requirement is satisfied by Co2+, is best supported by concentrations of divalent cation one-half the concentration of ATP440154
Co2+Azotobacter vinelandii-can replace Mg2+, but is less effective440158
Cu2+Klebsiella pneumoniae-1.4 gatom per mol of MoFe protein440149
FeAzotobacter vinelandii-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, overview714796
FeKlebsiella pneumoniae-in the active site iron-molybdenum cofactor, and as 4Fe-4S cluster in the Fe protein715017
Fe2+Azotobacter vinelandii-divalent cation requirement is satisfied by Fe2+, is best supported by concentrations of divalent cation one-half the concentration of ATP440154
Fe2+Azotobacter vinelandii-can replace Mg2+, but is less effective440158
Fe2+Methanococcus maripaludis-as part of the Fe protein in the MoFe protein, [4Fe-4S] clusters684881
Fe2+Klebsiella pneumoniae-nitrogenase Fe protein, the FeS cluster exhibits very little change upon MgATP binding, two bound nucleotides are believed to mediate the diverse, functionally essential structural rearrangements in the Fe protein687822
Fe2+Klebsiella pneumoniae-different VO2+-nucleotide coordination environments exist for the Fe-protein Kp2 that depend on pH and are distinguishable by EPR spectroscopy, Kp2 structure, overview687823
Fe2+Azotobacter vinelandii-in [Fe-S] clusters688191
Fe2+Azotobacter vinelandii-part of the iron-molybdenum and molybdenum-iron cofactors689764
Fe2+Anabaena sp.--713837
IronAzospirillum sp., Chlorobium sp., Desulfovibrio sp., Leptolyngbya boryana, Rhizobium leguminosarum, Rhodobacter sphaeroides, Rhodopseudomonas sp.--440134
IronAllochromatium vinosum-enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
IronAzotobacter vinelandii-enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex; iron content of MoFe protein: 30; the MoFe protein contains 2 molybdenum, about 30 iron and 30 inorganic sulphur atoms, 16 of the 30 Fe atoms are associated with S2- in four cubic [4Fe-4S] clusters, the remaining metal atoms are arranged in two copies of a cofactor called FeMo cofactor, FeMoCo, with a minimum stoichiometry of MoFe6S8-9440142
IronKlebsiella pneumoniae-enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
IronRhodobacter capsulatus-2.7-4.1 mol per mol of Fe protein; 27.7 atoms of iron per molecule of MoFe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
IronRhodospirillum rubrum-20 atoms of iron per molecule of MoFe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
IronAllochromatium vinosum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae-17-19 atoms of iron per molecule of MoFe protein, overview440143
IronRhizobium lupini--440143
IronAllochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens-18-36 atoms of iron per molecule of MoFe protein , overview440145
IronDesulfovibrio desulfuricans-18-36 atoms of iron per molecule of MoFe protein , overview; iron content of the iron protein: 3.5440145
IronEscherichia coli, Gloeocapsa sp., Klebsiella pneumoniae, Leptolyngbya boryana, Ornithopus sativus, Paenibacillus polymyxa, Rhizobium lupini, Rhizobium sp., Rhodospirillum rubrum-18-36 atoms of iron per molecule of MoFe protein , overview440145
IronAzotobacter vinelandii, Klebsiella pneumoniae-4 atoms of iron per molecule of Fe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440147
IronKlebsiella pneumoniae-17.5 gatom per mol of MoFe protein; 4 atoms of iron per molecule of Fe protein440149
IronAzotobacter vinelandii-characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins440156
IronAzospirillum amazonense-24 atoms of iron per molecule of MoFe protein440161
IronRhizobium sp.-22.5 atoms of iron per molecule of protein; 3.1440162
IronRhizobium lupini-4 atoms of iron per molecule of Fe protein440165
IronAnabaena sp.--440134, 440166
IronAnabaena variabilis, Azospirillum brasilense--440166
IronAzotobacter chroococcum--440143, 440146, 440166
IronAzotobacter sp., Frankia sp., Gloeothece sp.--440134, 440166
IronOscillatoria sp.--440166
IronRhodospirillum rubrum--440134, 440143, 440166
IronAzotobacter chroococcum-4 atoms of iron per molecule of Fe protein440167
IronXanthobacter autotrophicus--440168
IronPaenibacillus polymyxa--440134, 440143, 440146, 440147, 440169
IronAnabaena cylindrica--440134, 440170
IronRhodobacter capsulatus--440171
IronChromatium sp.--440134, 440174
IronClostridium pasteurianum--440134, 440142, 440146, 440147, 440159, 440174
IronKlebsiella pneumoniae--440134, 440146, 440157, 440166, 440174
IronRhizobium sp.--440134, 440166, 440174
IronRhodobacter capsulatus-the iron-only enzyme consists of 2 components: Fe protein and FeFe protein, the latter contains 26 Fe atoms per molecul of protein440176
IronAzotobacter vinelandii, Clostridium pasteurianum-contains [4Fe4S] cluster; reduction kinetics440180
IronAzotobacter vinelandii--440134, 440138, 440146, 440158, 440166, 440174, 440175, 440181, 440182
IronAzotobacter chroococcum-contains [4Fe4S] cluster440186
IronAzotobacter vinelandii-contains [4Fe4S] cluster440179, 440183, 440186
IronClostridium pasteurianum-contains [4Fe4S] cluster440186
IronAzotobacter vinelandii-contains [4Fe4S] cluster; VFe protein form 1 is an incomplete form that contains only 1 cofactor and 1 [4Fe-4S] cluster with an additional [Fe4-S4]-like cluster440188
IronRhodobacter capsulatus-required, part of the MoFe protein cofactor657985
IronAzotobacter vinelandii-dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the enzyme complex contains also a dimeric iron protein658010
IronAzotobacter vinelandii-enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, 1 of 2 different models proposes one or more Fe atoms in the Mo cofactor to be responsible for substrate binding658040
IronAzotobacter vinelandiiP00459dependent on, the enzyme complex contains a molybdenum-iron, a tetramer with 2 different subunits and 4 organo-metallic clusters, i.e. 2 iron-molybdenum cofactors and 2 P-clusters encoded by the genes nifD and nifK, the enzyme complex contains also a dimeric iron protein, encoded by the nifH gene, with a [4Fe4S] cluster between subunits and 2 MgATP binding sites, mechanism of electron transfer between metal clusters, mechanism of switch I and II, complex formation with the MoFe protein, also between different species, overview658483
IronHerbaspirillum seropedicae-dependent on, the enzyme complex contains a molybdenum-iron, a tetramer with 2 different subunits and 4 organo-metallic clusters, i.e. 2 iron-molybdenum cofactors and 2 P-clusters, the enzyme complex contains also a homodimeric iron protein encoded by the nifH gene658769
IronKlebsiella pneumoniae-dependent on, the enzyme complex contains a molybdenum-iron protein, and a dimeric iron protein658901
IronAzotobacter vinelandii-enzyme contains an iron-molybdenum cofactor659338
IronAzotobacter vinelandii-freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate in mutant V70A/H195Q. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor672039
IronGluconacetobacter diazotrophicus-component Gd1, iron and molybdenum in a 12:1 ratio. Component Gd2, 3.9 Fe atoms per molecule672344
IronAzotobacter vinelandiiP07328in FeMo cofactor and MoFe protein715813
IronAzotobacter vinelandii-in the MoFe protein and the Fe protein716922
IronAzotobacter vinelandii-in the FeMo cofactor716924
Mg2+Anabaena cylindrica, Anabaena sp., Azospirillum sp., Azotobacter sp., Chlorobium sp., Chromatium sp., Clostridium pasteurianum, Desulfovibrio sp., Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Leptolyngbya boryana, Paenibacillus polymyxa, Rhizobium leguminosarum, Rhizobium sp., Rhodobacter sphaeroides, Rhodopseudomonas sp., Rhodospirillum rubrum--440134
Mg2+Allochromatium vinosum, Anabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens-Mg2+ required for MgATP complex440144, 440145
Mg2+Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus-Mg2+ required for MgATP complex440145
Mg2+Rhizobium lupini-Mg2+ required for MgATP complex440144, 440145
Mg2+Paenibacillus polymyxa-Mg2+ required for MgATP complex440144, 440145, 440146, 440147
Mg2+Klebsiella pneumoniae-1.8 gatom per mol of MoFe protein; Mg2+ required for MgATP complex440149
Mg2+Azotobacter vinelandii-divalent metal requirement is satisfied by Mg2+, reaction is best supported by concentration of divalent cation one-half the concentration of ATP440154
Mg2+Anabaena sp., Anabaena variabilis, Azospirillum brasilense, Azotobacter sp., Frankia sp., Gloeothece sp., Oscillatoria sp.-Mg2+ required for MgATP complex440166
Mg2+Rhodospirillum rubrum-Mg2+ required for MgATP complex440144, 440145, 440166
Mg2+Chromatium sp.-Mg2+ required for MgATP complex440174
Mg2+Klebsiella pneumoniae-Mg2+ required for MgATP complex440144, 440145, 440146, 440147, 440157, 440166, 440174
Mg2+Rhizobium sp.-Mg2+ required for MgATP complex440145, 440166, 440174
Mg2+Azotobacter chroococcum-Mg2+ required for MgATP complex440144, 440145, 440146, 440166, 440186
Mg2+Clostridium pasteurianum-Mg2+ required for MgATP complex440144, 440145, 440146, 440147, 440164, 440174, 440180, 440186
Mg2+Azotobacter vinelandii-Mg2+ required for MgATP complex440138, 440144, 440145, 440146, 440147, 440158, 440166, 440174, 440175, 440178, 440180, 440182, 440184, 440186, 440187
Mg2+Azotobacter vinelandiiP00459required for ATP binding and MgATP hydrolysis, 2 MgATP binding sites on the iron protein connected via residues K15, D125, and C132, binding changes the conformation and the redox status of the [4Fe4S] cluster of the iron protein, mechanism, overview658483
Mg2+Klebsiella pneumoniae-required, the FeS cluster exhibits very little change upon MgATP binding687822
Mg2+Azotobacter vinelandii--440134, 658010, 659426, 688191, 689764
Mg2+Azotobacter vinelandii-MgATP2- is required714796
Mg2+Azotobacter vinelandii-required715263
Mn2+Azotobacter vinelandii-divalent cation requirement is satisfied by Mn2+, is best supported by concentrations of divalent cation one-half the concentration of ATP440154
Mn2+Azotobacter vinelandii-can replace Mg2+, but is less effective440158
MoAzotobacter vinelandii-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-subunit714796
MoKlebsiella pneumoniae-in the active site iron-molybdenum cofactor715017
MolybdenumAzospirillum sp., Chlorobium sp., Chromatium sp., Desulfovibrio sp., Leptolyngbya boryana, Rhizobium leguminosarum, Rhodobacter sphaeroides, Rhodopseudomonas sp.--440134
MolybdenumAllochromatium vinosum-enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex440142
MolybdenumAzotobacter vinelandii-2 gatom per mol of MoFe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex440142
MolybdenumKlebsiella pneumoniae-enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex440142
MolybdenumRhodobacter capsulatus-1.2-1.3 gatom per mol of MoFe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex440142
MolybdenumRhodospirillum rubrum-1.7 gatom per mol of MoFe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex440142
MolybdenumAllochromatium vinosum-1-2 gatom per mol of MoFe protein , overview440143, 440145
MolybdenumAnabaena cylindrica-1-2 gatom per mol of MoFe protein , overview440145
MolybdenumBradyrhizobium japonicum-1-2 gatom per mol of MoFe protein , overview440143, 440145
MolybdenumCorynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus-1-2 gatom per mol of MoFe protein , overview440145
MolybdenumRhizobium lupini-1-2 gatom per mol of MoFe protein , overview440143, 440145
MolybdenumRhizobium sp.-1-2 gatom per mol of MoFe protein , overview440145
MolybdenumRhodospirillum rubrum-1-2 gatom per mol of MoFe protein , overview440143, 440145
MolybdenumAzotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa-1-2 gatom per mol of MoFe protein , overview440143, 440145, 440146
MolybdenumAzotobacter vinelandii-enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex; molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview; review on molybdenum in nitrogenase440147
MolybdenumClostridium pasteurianum-molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview; review on molybdenum in nitrogenase440147
MolybdenumKlebsiella pneumoniae-6 iron atoms to 1 molybdenum atom in MoFe protein; enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex; molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview; review on molybdenum in nitrogenase440147
MolybdenumPaenibacillus polymyxa-review on molybdenum in nitrogenase440147
MolybdenumCyanobacterium sp.-enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex440148
MolybdenumKlebsiella pneumoniae-1 gatom per mol of MoFe protein440149
MolybdenumAzotobacter vinelandii-also possesses Mo-independent nitrogenases: one vanadium containing nitrogenase and another lacking both molybdenum and vanadium440150, 440155
MolybdenumAzotobacter vinelandii-characterization of the metal clusters in the nitrogenase molybdenum-iron protein440156
MolybdenumClostridium pasteurianum--440134, 440142, 440159
MolybdenumAzospirillum amazonense-2 gatom per mol of MoFe protein440161
MolybdenumRhizobium sp.-1.2-1.3 gatom per mol of MoFe protein440162
MolybdenumRhizobium lupini--440165
MolybdenumAnabaena variabilis--440148, 440166
MolybdenumAzospirillum brasilense--440166
MolybdenumAzotobacter chroococcum--440150, 440166
MolybdenumAzotobacter sp., Frankia sp., Gloeothece sp.--440134, 440166
MolybdenumKlebsiella pneumoniae--440134, 440157, 440166
MolybdenumOscillatoria sp.--440166
MolybdenumRhizobium sp., Rhodospirillum rubrum--440134, 440166
MolybdenumAzotobacter chroococcum-23 mol Fe + 1.9 mol Mo per mol of MoFe protein440167
MolybdenumXanthobacter autotrophicus--440168
MolybdenumPaenibacillus polymyxa--440134, 440169
MolybdenumAnabaena cylindrica--440134, 440170
MolybdenumRhodobacter capsulatus--440171
MolybdenumAzotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.-molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview440174
MolybdenumAzotobacter vinelandii-mol Mo per mol MoFeprotein: wild-type and mutant H195Q 1.9, mutant H195N and Q191K 0.9440181
MolybdenumAzotobacter vinelandii--440134, 440138, 440158, 440166, 440175, 440179, 440182, 440183
MolybdenumAzotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum-MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands440186
MolybdenumRhodobacter capsulatus-required, part of the MoFe protein cofactor, can be partially, about 25%, substituted by tungsten, Mo content quantification, overview, Mo cannot be substituted by rhenium657985
MolybdenumAzotobacter vinelandii-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 analysis658010
MolybdenumAzotobacter vinelandii-enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, where X can be an N atom, 1 of 2 different models proposes molydenum as the substrate binding partner in the active site658040
MolybdenumAzotobacter vinelandiiP00459dependent on, the enzyme complex contains a molybdenum-iron, a tetramer with 2 different subunits and 4 organo-metallic clusters, i.e. 2 iron-molybdenum cofactors [7Fe-Mo-9S-X-homocitrate] and 2 P-clusters [8Fe-7S], mechanism of electron transfer between metal clusters, complex formation with the Fe protein, also between different species, overview658483
MolybdenumHerbaspirillum seropedicae-dependent on, the enzyme complex contains a molybdenum-iron, a tetramer with 2 different subunits and 4 organo-metallic clusters, i.e. 2 iron-molybdenum cofactors and 2 P-clusters658769
MolybdenumKlebsiella pneumoniae-dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site658901
MolybdenumAzotobacter vinelandii-enzyme contains an iron-molybdenum cofactor659338
MolybdenumAzotobacter vinelandii-freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate in mutant V70A/H195Q. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor672039
MolybdenumGluconacetobacter diazotrophicus-component Gd1, iron and molybdenum in a 12:1 ratio, molybdenum content is 1.4 atoms per enzyme tetramer672344
MolybdenumAzotobacter vinelandii-part of the iron-molybdenum and molybdenum-iron cofactors689764
MolybdenumAnabaena sp.--440134, 440166, 713837
MolybdenumAzotobacter chroococcum-in the FeMoco cofactor of the MoFe protein715261
MolybdenumAzotobacter vinelandiiP07328in FeMo cofactor and MoFe protein715813
MolybdenumAzotobacter vinelandii-in the MoFe protein716922
Ni2+Azotobacter vinelandii-divalent cation requirement is satisfied by Ni2+, is best supported by concentrations of divalent cation one-half the concentration of ATP440154
Ni2+Azotobacter vinelandii-can replace Mg2+, but is less effective440158
TungstenRhodobacter capsulatus-can partially, about 25%, substitute for molybdenum, isolation of a tungsten-substituted enzyme after growth of the cells in tungsten-supplemented and molybdenum-deficient medium657985
VanadiumAzotobacter chroococcum-possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium440150
VanadiumAzotobacter vinelandii-possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium440150, 440155
VanadiumAzotobacter chroococcum-characterization of the metal clusters in the nitrogenase vanadium-iron protein440186
VanadiumAzotobacter vinelandii-characterization of the metal clusters in the nitrogenase vanadium-iron protein440156, 440186
VanadiumClostridium pasteurianum-characterization of the metal clusters in the nitrogenase vanadium-iron protein440186
VanadiumAzotobacter vinelandii-2 forms of VFe protein: form 1 has V-toFe ratio of 1:19, form 2 of 1:15; VFe protein form 1 is an incomplete form that contains only 1 cofactor and 1 [4Fe-4S] cluster with an additional [Fe4-S4]-like cluster440188
VanadiumAzotobacter chroococcum-in the FeVco cofactor715261
Zn2+Klebsiella pneumoniae-0.8 gatom per mol of MoFe protein440149
MolybdenumAzotobacter vinelandii-in the FeMo cofactor716924
additional informationAnabaena cylindrica, Anabaena sp., Azospirillum sp., Azotobacter sp., Azotobacter vinelandii, Chlorobium sp., Chromatium sp., Clostridium pasteurianum, Desulfovibrio sp., Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Leptolyngbya boryana, Paenibacillus polymyxa, Rhizobium leguminosarum, Rhizobium sp., Rhodobacter sphaeroides, Rhodopseudomonas sp., Rhodospirillum rubrum-metal-sulfur cluster, e.g. [4Fe-4S]440134
additional informationAllochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum-other metal ions, e.g. Cu2+, Mg2+, Zn2+, Ca2+, at levels of 1-2 atoms per mol detected in the MoFe protein, no evidence for specific requirement, except for Mg2+ in MgATP complex, of any of these metals440144
additional informationAzotobacter chroococcum--440150
additional informationAzotobacter vinelandii--440150, 440174
additional informationChromatium sp.--440174
additional informationClostridium pasteurianum-contains also an inactive MoFe protein species440174
additional informationKlebsiella pneumoniae, Rhizobium sp.--440174
additional informationRhodobacter capsulatus-the iron-only nitrogenase form contains no molybdenum, vanadium or any other heterometal atom440176
additional informationRhodobacter capsulatus-redox properties of metal clusters440177
additional informationAzotobacter chroococcum, Clostridium pasteurianum-structure and organization of metal clusters440186
additional informationAzotobacter vinelandii-structure and organization of metal clusters440186, 440188, 440189
additional informationRhodobacter capsulatus-rhenium cannot substitute for molybdenum in vitro, nor in vivo657985
additional informationAzotobacter vinelandiiP00459structure catalytic role, and mechanism of the P-cluster, part of the MoFe protein, which has a role in immediate electron acceptance from the Fe protein658483
additional informationAzotobacter vinelandii-structures of the metal centers in Fe protein and MoFe protein, overview714796

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,10-phenanthrolineAzotobacter vinelandii--440154 2D-image
1,2-Dihydroxybenzene 3,5-disulfonateAzotobacter vinelandii--440154 2D-image
2,2'-dipyridylAzotobacter vinelandii--440154 2D-image
2,3-DimercaptopropanolAzotobacter vinelandii--440154 2D-image
AcetyleneAzotobacter vinelandii-noncompetitive inhibition of N2 reduction658040 2D-image
AcetyleneAzotobacter vinelandiiP00459noncompetitive inhibition of nitrogen reduction, Gly69 is important658483 2D-image
ADPAzotobacter vinelandii--440154 2D-image
ADPAzotobacter vinelandii-above 5 mM440158 2D-image
ATPAzotobacter vinelandii--440158 2D-image
beryllium fluorideAzotobacter vinelandiiP00459inhibits by trapping of a stable Fe protein-MoFe protein nitrogenase complex658483 2D-image
C2H2Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa-noncompetitive inhibitor of N2 reduction440146 2D-image
C2H2Azotobacter vinelandii-inhibition of H195 mutants440180 2D-image
C2H2Clostridium pasteurianum--440180 2D-image
C2H2Azotobacter vinelandii-competitive to N2440183 2D-image
Ca2+Azotobacter vinelandii--440158 2D-image
COAzotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa-noncompetitive inhibitor of N2, C2H2 and N3- reduction, no inhibition of H+ reduction440146 2D-image
COClostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa--440147 2D-image
COAzotobacter vinelandii-inhibition of CH4 and NH3 production from CN-440181 2D-image
COAzotobacter vinelandii-inhibition of H+ reduction by about 50%440189 2D-image
COAzotobacter vinelandii-binds to the active site658010 2D-image
COAzotobacter vinelandii--440147, 440154, 440158, 440183, 658040 2D-image
COAzotobacter vinelandiiP00459strong inhibition, binding site and inhibition mechanism658483 2D-image
Cu2+Azotobacter vinelandii--440154 2D-image
cyanideAzotobacter vinelandiiP00459-658483 2D-image
cyanideKlebsiella pneumoniae-inhibits electron flow658901 2D-image
glutamineRhodobacter capsulatus, Rhodospirillum rubrum--440142 2D-image
H2Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Rhizobium lupini, Rhodospirillum rubrum--440144 2D-image
H2Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum-competitive inhibitor of N2, no inhibition of N3-, C2H2, CN- or H+ reduction440146 2D-image
H2Klebsiella pneumoniae, Paenibacillus polymyxa--440144, 440146 2D-image
H2Azotobacter vinelandii--440144, 440154, 440158 2D-image
H2Azotobacter vinelandii-competitive440183 2D-image
H2Azotobacter vinelandii-competitive inhibition of N2 binding658040 2D-image
hydrazineAzotobacter vinelandii-and derivatives440158 2D-image
L-asparagineGluconacetobacter diazotrophicus-76% inhibition at 10 mM asparagine in the growth medium658372 2D-image
L-aspartic acidGluconacetobacter diazotrophicus-67% inhibition at 10 mM aspartic acid in the growth medium658372 2D-image
L-cysteineGluconacetobacter diazotrophicus-51% inhibition at 5 mM cysteine in the growth medium658372 2D-image
L-Glutamic acidGluconacetobacter diazotrophicus-68% inhibition at 10 mM glutamic acid in the growth medium658372 2D-image
L-glutamineGluconacetobacter diazotrophicus-60% inhibition at 10 mM glutamine in the growth medium658372 2D-image
L-leucineGluconacetobacter diazotrophicus-54% inhibition at 5 mM leucine in the growth medium658372 2D-image
N2Azotobacter vinelandii-inhibits C2H2 reduction of mutant H195Q; maximal inhibition of H2 production at Fe protein to MoFe protein ration 2.5440184 2D-image
N2Azotobacter vinelandii-inhibits the C2H2 reduction440183, 440189 2D-image
N2Azotobacter vinelandii-competitive inhibition of acetylene reduction658040 2D-image
N2Azotobacter vinelandii-inhibits hydrazine reduction659426 2D-image
N3-Azotobacter vinelandii-inhibits H2 production competitively and reversibly440184 2D-image
NaClGluconacetobacter diazotrophicus-half-maximal inhibition at 100 mM672344 2D-image
NAD+-malic enzymeMesorhizobium loti-affects nitrogenase activity of Mesorhizobium loti bacteroids in Lotus japonicus nodules, also in Bradyrhizobium japonicum and Sinorhizobium meliloti. nodules, analysis by signature-tagged mutagenesis using transposon insertion malic enzyme mutants, overview716483-
NH4+Rhodobacter capsulatus, Rhodospirillum rubrum-immediate inhibition, repression of induction440142 2D-image
NH4+Beggiatoa alba-immediate inhibition, repression of induction440160 2D-image
NH4+Gluconacetobacter diazotrophicus-18% inhibition at 5 mM, 32% at 15 mM ammonium in the growth medium658372 2D-image
NH4ClAzoarcus sp.-nitrogenase activity is repressed by the addition of 0.5 mM NH4Cl698619 2D-image
NIFI1,2Methanococcus maripaludis-a regulatory protein, inhibits nitrogenase by competing with Fe protein for binding to the MoFe protein, NifI1,2 inhibits ATP- and MoFe protein-dependent oxidation of the Fe protein, and NIFI1,2 binding prevents association of the two nitrogenase components, the inhibition is relieved by 2-oxoglutarate. NIFI1,2 is unable to bind to an AlF4-stabilized Fe protein-MoFe protein complex. Both nifI1 and nifI2 are required for regulation in vivo684881-
nitrateLotus japonicus-involvement of NO production in the inhibition of nitrogenase activity by nitrate , overview. The enzyme of plant symbiont Mesorhizobium loti, strain New Zealand Palmerston 2235, is not inhibited by nitrate699812-
NOAzotobacter vinelandii--440154 2D-image
NO3-Gluconacetobacter diazotrophicus-17% inhibition at 15 mM nitrate in the growth medium658372 2D-image
O2Klebsiella pneumoniae-complete reversible inhibition, reversibility decreases by increasing the time of exposure to O2440140 2D-image
O2Clostridium pasteurianum--440142, 440147 2D-image
O2Paenibacillus polymyxa--440147 2D-image
O2Cyanobacterium sp.-irreversibly inactivated440148 2D-image
O2Klebsiella pneumoniae--440142, 440147, 440149 2D-image
O2Azotobacter vinelandii--440142, 440147, 440154 2D-image
phosphateAzotobacter vinelandii-above 30 mM440158 2D-image
SCN-Azotobacter vinelandii-above 6 mM occurs substrate inhibition440178 2D-image
sodium nitroprussideLotus japonicus-influence of the NO donor sodium nitroprusside on the relative levels of acetylene reduction activity, overview699812 2D-image
tetrafluoroaluminateAzotobacter vinelandiiP00459inhibits by trapping of a stable Fe protein-MoFe protein nitrogenase complex, binds to the Fe protein658483 2D-image
tungstateRhodobacter capsulatus-30% inhibition at 0.01 mM, 50% inhibition at 0.1 mM, 95% inhibition at 1 mM, inhibits MoFe protein expression657985 2D-image
UreaBeggiatoa alba-immediate inhibition, repression of induction440160 2D-image
VanadiumAzotobacter vinelandii-contains 3 classes of nitrogenase, the second contains V, the third is encoded by a separate set of genes and is inhibited by V and Mo440150 2D-image
VO2+Klebsiella pneumoniae-structural basis for VO2+ inhibition of nitrogenase activity, 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy, vanadyl hyperfine couplings of VO2+-ATP and VO2+-ADP complexes in the presence of the nitrogenase Fe protein, overview687822 2D-image
Zn2+Azotobacter vinelandii--440154 2D-image
MgADPAzotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa--440146 2D-image
additional informationAzotobacter vinelandii-high ionic strength inhibits440154-
additional informationAzotobacter vinelandii-e.g. above 50 mM NaCl; high ionic strength inhibits440158-
additional informationAzotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae-overview440174-
additional informationGluconacetobacter diazotrophicus-enzyme activity and bacterial growth is affected by amino acids in the growth medium658372-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
C2H2Azotobacter vinelandii-enhances the CH4 production but not NH3 production from CN-, wild-type enzyme440181 2D-image
homocitrateAzotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum-plays role in electron transfer at the [4Fe-4S] cluster to the MoFe-cofactor of the MoFe protein, can be substituted by erythro-fluorohomocitrate but not by threo-fluorohomocitrate440186 2D-image
lightAzotobacter vinelandii-light-driven activation of the molybdenum-iron-protein, MoFeP, of nitrogenase for substrate reduction is independent of ATP hydrolysis and the iron-protein, FeP, binding structure and mechanism, overview715263-
molybdateRhodobacter capsulatus-induces MoFe protein expression657985 2D-image
additional informationRhodospirillum rubrum-Fe protein contains an adenine-like molecule, a pentose moiety and a phosphate residue covalently attached to the molecule440142-
additional informationRhodobacter capsulatus-Fe protein contains an adenine-like molecule, a pentose moiety and a phosphate residue covalently attached to the molecule440142, 440171-
additional informationAzotobacter vinelandii-H2 generation activates N2 binding658040-
additional informationBradyrhizobium japonicum-several organic acids highly stimulate the enzyme activity of anaerobically isolated bacteroids, only malate has little effect660287-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.3-ATPAzotobacter vinelandii--440154 2D-image
0.3-ATPAzotobacter vinelandii-with C2H2440158 2D-image
0.3-C2H2Azotobacter vinelandii--440158 2D-image
0.41.2C2H2Azotobacter vinelandii--440154 2D-image
0.45-CH4Azotobacter vinelandii-mutant H195Q440181 2D-image
1.6-CH4Azotobacter vinelandii-wild-type440181 2D-image
4.5-CH4Azotobacter vinelandii-mutant H195N440181 2D-image
0.1-N2Azotobacter vinelandii--440154 2D-image
0.1-N2Azotobacter vinelandii-with C2H2440158 2D-image
0.9-SCN-Azotobacter vinelandii--440178 2D-image
12-CH4Azotobacter vinelandii-mutant Q191K440181 2D-image
additional information-additional informationAllochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae--440144-
additional information-additional informationAzotobacter vinelandii--440154-
additional information-additional informationAnabaena cylindrica--440170-
additional information-additional informationAzotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae-overview, different substrates440174-
additional information-additional informationRhodobacter capsulatus--440176-
additional information-additional informationAzotobacter vinelandii--440183, 440184, 440189-
additional information-additional informationRhodobacter capsulatus-EPR signals of Mo and of W containing cofactor, redox potentials657985-
additional information-additional informationAzotobacter vinelandii-determination of EPR signals of wild-type enzyme and V70A mutant MoFe protein-containing enzyme with propargyl alcohol and C2H2 as substrates, temperature dependence658010-
additional information-additional informationAzotobacter vinelandiiP00459redox properties of metal clusters and P-cluster, overview658483-
additional information-additional informationKlebsiella pneumoniae-reaction kinetics for the isolated MoFe protein in reaction with cyanide with ligands tert-butylcyanide, butyl isocyanide, or imidazole, bound to the cofactor protein, cyanide binding kinetics, stopped-flow measurements658901-
additional information-additional informationAzotobacter vinelandii-Km for N2 of wild-type and mutant enzyme659426-
additional information-additional informationAzotobacter vinelandii-kinetic analysis, overview689764-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.3-SCN-Azotobacter vinelandii--440178 2D-image
400-flavodoxin hydroquinoneAzotobacter vinelandii-before and after reduction of the nitrogenase complex relatively slow reactions take place, which limits the rate of the Fe protein cycle440138-
additional information-additional informationAzotobacter vinelandii-1200 per min: proton production of the reduced enzyme, MgATP-dependent440175-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
10.1-SCN-Azotobacter vinelandii--440178 2D-image
additional information-additional informationAzotobacter vinelandii--440184, 440189-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.024-Azotobacter vinelandii-purified mutant H195Q enzyme, anaerobic atmosphere440184
0.027-Klebsiella pneumoniae-reductant dithionite, whole cell assay440140
0.066-Azotobacter vinelandii-crude extract, 100% Ar atmosphere, H2 production440189
0.13-Azotobacter vinelandii-V70I mutant, substrate acetylene, in presence of C2H4659426
0.17-Azotobacter vinelandii-V70I mutant, substrate N2, in presence of NH3659426
0.2-Azotobacter vinelandii-wild-type enzyme, substrate acetylene, in presence of H2659426
0.235-Rhodobacter capsulatus-substrate N2, purified Mo nitrogenase440176
0.26-Rhodobacter capsulatus-substrate C2H2, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1440176
0.27-Azotobacter vinelandii-mutant A175G, purified enzyme, substrate C2H2440182
0.35-Rhodobacter capsulatus-substrate N2, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1440176
0.43-Rhizobium lupini-purified Fe protein440165
0.60.8Rhodobacter capsulatus-purified Fe protein440171
0.6-Azotobacter vinelandii-wild-type enzyme, substrate N2, in presence of NH3659426
0.64-Azotobacter vinelandii-wild-type enzyme, substrate N2, in presence of H2659426
0.7-Rhizobium lupini-purified MoFe protein440165
0.7-Azotobacter vinelandii-purified enzyme, anaerobic atmosphere440184
1.01-Azotobacter vinelandii-purified MoFe protein440163
1.07-Xanthobacter autotrophicus-purified MoFe protein440168
1.2-Clostridium pasteurianum-purified MoFe protein440159
1.2-Rhodobacter capsulatus-substrate C2H2, purified Mo nitrogenase440176
1.26-Xanthobacter autotrophicus-purified Fe protein440168
1.3-Rhodobacter capsulatus-substrate H+, purified Mo nitrogenase440176
1.51.7Rhodobacter capsulatus-purified MoFe protein440171
1.52-Azotobacter vinelandii-wild-type, purified enzyme, substrate C2H2440182
1.6-Gluconacetobacter diazotrophicus-30C, pH 7.5672344
1.72.2Clostridium pasteurianum-purified Fe protein440159
1.8-Azospirillum amazonense-purified Fe protein440161
1.8-Azotobacter vinelandii-wild-type enzyme, substrate acetylene, in presence of C2H4659426
1.94-Azotobacter vinelandii-V70I mutant, substrate N2, in presence of H2659426
2-Azotobacter vinelandii-wild-type enzyme, C2H2 reduction658010
2-Azotobacter vinelandii-V70I mutant, substrate acetylene, in presence of H2659426
2.01-Azotobacter vinelandii-purified Fe protein440163
2.02-Azotobacter vinelandii-wild-type enzyme, substrate argon, in presence of H2659426
2.082-Klebsiella pneumoniae-purified component II440157
2.16-Klebsiella pneumoniae-purified component I440157
2.2-Azotobacter vinelandiiP07328about, micromol/min/mg MoFe protein, mutant enzyme, pH not specified in the publication, temperature not specified in the publication715813
2.272.28Azotobacter vinelandii-purified enzyme, substrate acetylene440178
2.316-Azotobacter vinelandiiP07328about, micromol/min/mg MoFe protein, wild-type enzyme, pH not specified in the publication, temperature not specified in the publication715813
2.34-Azotobacter vinelandii-V70I mutant, substrate argon, in presence of H2659426
2.4-Azospirillum amazonense-purified MoFe protein440161
2.4-Rhodobacter capsulatus-substrate H+, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1440176
additional information-Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii-activity of Fe proteins and MoFe proteins440143
additional information-Bradyrhizobium japonicum--440143
additional information-Clostridium pasteurianum, Klebsiella pneumoniae-activity of Fe proteins and MoFe proteins440143
additional information-Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum--440143
additional information-Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum--440144
additional information-Klebsiella pneumoniae--440149
additional information-Azotobacter vinelandii--440154, 440158
additional information-Rhizobium sp.--440162
additional information-Paenibacillus polymyxa--440169
additional information-Anabaena cylindrica--440170
additional information-Azotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.-activity of Fe proteins and MoFe proteins; overview440174
additional information-Rhodobacter capsulatus--440176
additional information-Azotobacter vinelandii-assay in anaerobic atmosphere required440182, 440184
additional information-Azotobacter vinelandii-assay in anaerobic atmosphere required; wild-type and diverse alpha-His195 MoFe protein mutants440189
additional information-Gluconacetobacter diazotrophicus-in vivo activity measurement, quantification of ethylene658372
additional information-Anabaena sp.-comparison of relative nitrogen-fixing ability, H2 production rates, and reduction rates of acetylene (under Ar) of wild-type and mutant NifD variants, overview713837
additional information-Klebsiella pneumoniae-comparison of ATP consumption coupled to H2 production by recombinant NifDK/NifB-co and by NifDK, overview715017
additional information-Azotobacter vinelandii-rates of ATP hydrolysis by Mo and V nitrogenases are comparable under CO, which reflected a similar flux of electrons through the two nitrogenases716922

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6.58Beggiatoa alba--440160
6.5-Azotobacter vinelandii-SCN- reduction440178
78Azotobacter vinelandii-assay at, hydrazine reduction activity659426
7-Azotobacter vinelandii-assay at658010
7-Azotobacter vinelandii-assay at, N2 reduction activity659426
7.17.3Xanthobacter autotrophicus-with substrates: N2, C2H2440168
7.3-Azotobacter vinelandii--440158
7.4-Klebsiella pneumoniae-assay at440157
7.4-Azotobacter vinelandii-assay at440163, 440181, 440182
7.5-Methanococcus maripaludis-assay at, acetylene reduction684881
8-Klebsiella pneumoniae-assay at658901

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
6.58.3Xanthobacter autotrophicus-pH 6.5: no activity below, pH 8.3: about 70% of activity maximum440168
6.58.5Rhodobacter capsulatus-below and above no remaining activity440176
7.3-Gluconacetobacter diazotrophicus-narrow range672344

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
1540Azotobacter vinelandii-no maximum with Ti3+ as reductant440180
25-Azotobacter vinelandii-assay at658010
25-Klebsiella pneumoniae-assay at658901
29-Beggiatoa alba--440160
30-Klebsiella pneumoniae-assay at440157
30-Azotobacter vinelandii-assay at440158
30-Azospirillum amazonense-assay at440161
30-Rhizobium sp.-assay at440162
30-Azotobacter vinelandii-assay at440163, 440180
30-Clostridium pasteurianum-assay at440180
30-Azotobacter vinelandii-assay at440181, 440182
30-Gluconacetobacter diazotrophicus-in vivo assay at658372
30-Azotobacter vinelandii-assay at659426
additional information-Azotobacter vinelandii--440184

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1345Azotobacter vinelandii--440184
1540Azotobacter vinelandii-no maximum with Ti3+ as reductant440180

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
root noduleAllochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae-bacteroid440143Manually annotated by BRENDA team
root noduleRhizobium lupini-bacteroid440143, 440165Manually annotated by BRENDA team
root noduleLotus japonicus--699812Manually annotated by BRENDA team
heterocystCyanobacterium sp.-in heterocysteous cyanobacteria exclusive site of N2 fixation during aerobic growth440148Manually annotated by BRENDA team
additional informationAnabaena sp.-the enzyme is localized to the microaerobic environment of heterocysts, a highly differentiated subset of the filamentous cells713837Manually annotated by BRENDA team
additional informationCrocosphaera watsonii-highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected, enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview714845Manually annotated by BRENDA team
additional informationGloeothece sp.-highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected 41C and above. Enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview714845Manually annotated by BRENDA team
additional informationMesorhizobium loti-cultivated as symbiont in Lotus japonicus root nodules716483Manually annotated by BRENDA team
additional informationAnabaena sp. PCC 7120-the enzyme is localized to the microaerobic environment of heterocysts, a highly differentiated subset of the filamentous cells-Manually annotated by BRENDA team
additional informationCrocosphaera watsonii WH8501-highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected, enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview-Manually annotated by BRENDA team
additional informationGloeothece sp. PCC6909-highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected 41C and above. Enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview-Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolLotus japonicus--5829699812Manually annotated by BRENDA team
additional informationAllochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum-not established, whether the nitrogenase exists in vivo in a specific particle or whether the nitrogenase proteins are bound nonspecifically to the membranes of some cells-440144Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1de0, downloadSCOP (1de0)CATH (1de0)Azotobacter vinelandii
1fp4, downloadSCOP (1fp4)CATH (1fp4)Azotobacter vinelandii
1fp6, downloadSCOP (1fp6)CATH (1fp6)Azotobacter vinelandii
1g1m, downloadSCOP (1g1m)CATH (1g1m)Azotobacter vinelandii
1g20, downloadSCOP (1g20)CATH (1g20)Azotobacter vinelandii
1g21, downloadSCOP (1g21)CATH (1g21)Azotobacter vinelandii
1g5p, downloadSCOP (1g5p)CATH (1g5p)Azotobacter vinelandii
1l5h, downloadSCOP (1l5h)CATH (1l5h)Azotobacter vinelandii
1m1n, downloadSCOP (1m1n)CATH (1m1n)Azotobacter vinelandii
1m1y, downloadSCOP (1m1y)CATH (1m1y)Azotobacter vinelandii
1m34, downloadSCOP (1m34)CATH (1m34)Azotobacter vinelandii
1n2c, downloadSCOP (1n2c)CATH (1n2c)Azotobacter vinelandii
1nip, downloadSCOP (1nip)CATH (1nip)Azotobacter vinelandii
1rw4, downloadSCOP (1rw4)CATH (1rw4)Azotobacter vinelandii
1xcp, downloadSCOP (1xcp)CATH (1xcp)Azotobacter vinelandii
1xd8, downloadSCOP (1xd8)CATH (1xd8)Azotobacter vinelandii
1xd9, downloadSCOP (1xd9)CATH (1xd9)Azotobacter vinelandii
1xdb, downloadSCOP (1xdb)CATH (1xdb)Azotobacter vinelandii
2afh, downloadSCOP (2afh)CATH (2afh)Azotobacter vinelandii
2afi, downloadSCOP (2afi)CATH (2afi)Azotobacter vinelandii
2afk, downloadSCOP (2afk)CATH (2afk)Azotobacter vinelandii
2c8v, downloadSCOP (2c8v)CATH (2c8v)Azotobacter vinelandii
2min, downloadSCOP (2min)CATH (2min)Azotobacter vinelandii
2nip, downloadSCOP (2nip)CATH (2nip)Azotobacter vinelandii
3k1a, downloadSCOP (3k1a)CATH (3k1a)Azotobacter vinelandii
3min, downloadSCOP (3min)CATH (3min)Azotobacter vinelandii
3u7q, downloadSCOP (3u7q)CATH (3u7q)Azotobacter vinelandii
4nd8, downloadSCOP (4nd8)CATH (4nd8)Azotobacter vinelandii
1cp2, downloadSCOP (1cp2)CATH (1cp2)Clostridium pasteurianum
1mio, downloadSCOP (1mio)CATH (1mio)Clostridium pasteurianum
1h1l, downloadSCOP (1h1l)CATH (1h1l)Klebsiella pneumoniae
1qgu, downloadSCOP (1qgu)CATH (1qgu)Klebsiella pneumoniae
1qh1, downloadSCOP (1qh1)CATH (1qh1)Klebsiella pneumoniae
1qh8, downloadSCOP (1qh8)CATH (1qh8)Klebsiella pneumoniae

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3500040000Azotobacter vinelandii-Fe protein440174
4000074000Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini-Fe protein: various methods, overview440143
4000074000Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini-Fe protein: various methods, overview440144
40000-Clostridium pasteurianum-Fe protein, ultracentrifugation440144
44000-Azotobacter vinelandii-FeMo cofactor-NafY protein complex, gel filtration659338
46000-Azotobacter vinelandii-NafY protein, gel filtration, sedimentation equilibrium centrifugation659338
51000-Bradyrhizobium japonicum-Fe protein, gel filtration440144
5500060000Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae-component II Fe protein440147
5500060000Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae-component II Fe protein440174
56000-Clostridium pasteurianum-Fe protein, gel filtration440144, 440164
60000-Cyanobacterium sp.-Fe protein440148
60000-Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum-about; Fe protein440186
61500-Rhodospirillum rubrum-Fe protein440142
62000-Klebsiella pneumoniae-Fe protein, gel filtration440144, 440149
63000-Azotobacter vinelandii-Fe protein440138, 440142
63000-Rhodobacter capsulatus-Fe protein440142, 440171
63000-Azotobacter vinelandii-Fe protein440187
64000-Azotobacter chroococcum, Azotobacter vinelandii-Fe protein, gel filtration440144
64000-Azotobacter chroococcum-Fe protein, gel filtration440167
65000-Rhizobium lupini-Fe protein, gel filtration440144, 440165
66800-Klebsiella pneumoniae-Fe protein440174
68200-Klebsiella pneumoniae-Fe protein, ultracentrifugation440144
74000-Rhizobium sp.-Fe protein, gel filtration440162
160000270000Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini-MoFe protein: various methods, overview440143
160000270000Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini-MoFe protein: various methods, overview440144
160000-Allochromatium vinosum-MoFe protein, estimation from Mo content, ultracentrifugation440144
168000-Clostridium pasteurianum-MoFe protein, ultracentrifugation440143
180000-Bradyrhizobium japonicum-MoFe protein, gel filtration440143
194000-Rhizobium lupini-MoFe protein, gel filtration440143, 440165
200000250000Rhodobacter capsulatus-tungsten-substituted enzyme component, gel filtration657985
200000-Bradyrhizobium japonicum--440143
200000-Clostridium pasteurianum-MoFe protein, gel filtration440143
200000-Klebsiella pneumoniae--440143
200000-Bradyrhizobium japonicum-MoFe protein, ultracentrifugation440144
200000-Clostridium pasteurianum--440144
200000-Klebsiella pneumoniae-MoFe protein, ultracentrifugation440144
210000-Clostridium pasteurianum-MoFe protein, gel filtration440164
216000-Azotobacter vinelandii-MoFe protein, gel filtration440143
216000-Cyanobacterium sp.-nitrogenase complex440148
219000-Rhizobium sp.-MoFe protein, gel filtration440162
220000250000Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae-component I MoFe protein440147
220000-Klebsiella pneumoniae-MoFe protein, gel filtration440149
220000-Anabaena cylindrica-MoFe protein, gel filtration440170
226000-Klebsiella pneumoniae-MoFe protein, gel filtration440143
227000-Azotobacter chroococcum-MoFe protein, gel filtration440167
230000-Azotobacter vinelandii-MoFe protein440138, 440142
230000-Rhodobacter capsulatus, Rhodospirillum rubrum-MoFe protein440142
230000-Rhodobacter capsulatus-MoFe protein440171
230000-Azotobacter vinelandii-MoFe protein440187
270000-Azotobacter vinelandii-MoFe protein, ultracentrifugation440143, 440144
additional information-Allochromatium vinosum, Azotobacter vinelandii-enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
additional information-Clostridium pasteurianum--440142
additional information-Klebsiella pneumoniae, Rhodobacter capsulatus, Rhodospirillum rubrum-enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
additional information-Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum--440145
additional information-Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa--440146
additional information-Klebsiella pneumoniae-enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440149
additional information-Clostridium pasteurianum--440159
additional information-Azospirillum amazonense--440161
additional information-Rhizobium lupini--440165
additional information-Azotobacter chroococcum--440167
additional information-Xanthobacter autotrophicus--440168
additional information-Paenibacillus polymyxa--440169
additional information-Rhodobacter capsulatus--440171
additional information-Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae-comparison of amino acid composition440174

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Azotobacter chroococcum-MoFe protein 4 * 60000 + Fe protein 2 * 30800, SDS-PAGE440167
?Rhodobacter capsulatus-FeFe protein of iron-only enzyme: 2 * 59000 + 2 * 51000 + 2 * 13500, alpha2beta2gamma2, SDS-PAGE; Fe protein of both enzyme forms: 2 * 30000-31000, gamma2, SDS-PAGE; MoFe protein: 2 * 59000 + 2 * 57000, alpha2beta2, SDS-PAGE440176
?Gluconacetobacter diazotrophicus-component Gd1, subunits of 53000 and 57500 Da, component Gd2, subunits of 33000 Da, SDS-PAGE672344
?Rhodobacter capsulatus B10S-FeFe protein of iron-only enzyme: 2 * 59000 + 2 * 51000 + 2 * 13500, alpha2beta2gamma2, SDS-PAGE; Fe protein of both enzyme forms: 2 * 30000-31000, gamma2, SDS-PAGE; MoFe protein: 2 * 59000 + 2 * 57000, alpha2beta2, SDS-PAGE-
dimerAllochromatium vinosum--440142, 440144
dimerAnabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens, Rhizobium lupini--440144
dimerRhodospirillum rubrum--440142, 440144
dimerAllochromatium vinosum-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440143, 440145
dimerAnabaena cylindrica-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440145
dimerAzotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440143, 440145
dimerCorynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp.-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440145
dimerKlebsiella pneumoniae-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440143, 440145
dimerLeptolyngbya boryana, Ornithopus sativus-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440145
dimerPaenibacillus polymyxa, Rhizobium lupini-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440143, 440145
dimerRhizobium sp.-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440145
dimerRhodospirillum rubrum-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview440143, 440145
dimerAzotobacter chroococcum--440144, 440146
dimerAzotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae--440142, 440144, 440146
dimerPaenibacillus polymyxa--440144, 440146
dimerRhizobium sp.-2 * 36000, SDS-PAGE440162
dimerClostridium pasteurianum-2 * 27500, SDS-PAGE440164
dimerAzotobacter vinelandii-2 * 26141-28000, unassociated NafY protein, sequence calculation and sedimentation equilibrium centrifugation659338
dimerAzotobacter vinelandii DJ-2 * 26141-28000, unassociated NafY protein, sequence calculation and sedimentation equilibrium centrifugation-
tetramerAllochromatium vinosum, Azotobacter vinelandii, Klebsiella pneumoniae-MoFe protein is an alpha2beta2-tetramer440142
tetramerRhodobacter capsulatus-alpha: 55000, beta: 59500; MoFe protein is an alpha2beta2-tetramer440142
tetramerRhodospirillum rubrum-alpha: 58500, beta: 58500; MoFe protein is an alpha2beta2-tetramer440142
tetramerAllochromatium vinosum, Anabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens--440144, 440145
tetramerDesulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus--440145
tetramerRhizobium lupini--440144, 440145
tetramerRhizobium sp.--440145
tetramerRhodospirillum rubrum--440144, 440145
tetramerAzotobacter chroococcum, Azotobacter vinelandii--440144, 440145, 440146
tetramerClostridium pasteurianum--440142, 440144, 440145, 440146
tetramerKlebsiella pneumoniae, Paenibacillus polymyxa--440144, 440145, 440146
tetramerCyanobacterium sp.--440148
tetramerRhizobium sp.-alpha: 56000, beta: 59000440162
tetramerClostridium pasteurianum-component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE440164
tetramerRhodobacter capsulatus-MoFe protein 1 * 55000 + 1 * 59000 + Fe protein 2 * 33500, SDS-PAGE440171
tetramerRhodobacter capsulatus--440176
tetramerRhodobacter capsulatus-tungsten-substituted enzyme component657985
tetramerCorynebacterium flavescens 301, Escherichia coli C-M 74, Rhodobacter capsulatus B10S---
dimerCorynebacterium flavescens 301, Escherichia coli C-M 74-Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview-
additional informationAzotobacter vinelandii-enzyme is composed of 2 metalloproteins: Fe protein and MoFe protein which are assumed to associate and dissociate to transfer a single electron to the substrates440138
additional informationAllochromatium vinosum, Azotobacter vinelandii, Klebsiella pneumoniae, Rhodobacter capsulatus, Rhodospirillum rubrum-enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex440142
additional informationAllochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Klebsiella pneumoniae, Rhizobium lupini, Rhodospirillum rubrum--440145
additional informationAzotobacter vinelandii-alpha-beta-monomer of the FeMo protein consists of the FeMo cofactor FeMo-co with the substrate reduction site and the [4Fe-4S] cluster440146
additional informationClostridium pasteurianum--440142, 440145, 440159
additional informationAzospirillum amazonense--440161
additional informationXanthobacter autotrophicus--440168
additional informationPaenibacillus polymyxa--440145, 440169
additional informationAnabaena cylindrica--440145, 440170
additional informationRhodobacter capsulatus--440171
additional informationAzotobacter vinelandii-apo-MoFe protein has a alpha2beta2 subunit composition and interacts with Fe protein, can be rebuilt by addition of FeMo-cofactor440179
additional informationAzotobacter vinelandii-VFe protein form 1 has alphabeta2 conformation, VFe protein form 2 has alpha2beta2 conformation440188
additional informationAzotobacter vinelandiiP00459overall enzyme complex structure with the MoFe protein, containing FeMo-cofactors and P-clusters, and 2 iron proteins, one with a [4Fe4S] cluster and MgATP, overview, components are encoded by the nif genes658483
additional informationAzotobacter vinelandii-the NafY protein monomerizes upon binding to the FeMo cofactor659338
additional informationGluconacetobacter diazotrophicus-enzyme consists of the two components Gd1 and Gd2, each containing two subunits. Half-amximal catalytic activity for Gd1 is reached at a Gd1/Gd2 ratio of 4:1672344
additional informationKlebsiella pneumoniae-Kp2 structure analysis bound to Vo2+, ATP, and ADP, characterization of the metal-nucleotide coordination environment, overview687822
additional informationKlebsiella pneumoniae-Kp2 structure analysis bound to Vo2+ and at different pH, overview687823
additional informationAzotobacter vinelandii-components of the electron transfer chains in nitrogenase and its homologue, overview714796
additional informationAzospirillum amazonense Y1---
additional informationAzotobacter vinelandii DJ-the NafY protein monomerizes upon binding to the FeMo cofactor-

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional informationMethanococcus maripaludis-model for posttranslational regulation of nitrogen fixation where the PII homologues Nifl1 and Nifl2 have an inhibitory effect on nitrogenase activity that is counteracted by high levels of 2-oxoglutarate, which acts as a signal of nitrogen limitation676049
additional informationRhodospirillum rubrum-posttranslational regulation of nitrogenase is mediated via GlnD, a bifunctional uridylyltransferase/uridylyl-removing enzyme which is important in nitrogen assimilation and metabolism662028

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Azotobacter vinelandii-440144, 440147
crystal structure analysis of the iron protein, and of the MoFe proteinAzotobacter vinelandiiP00459658483
crystallized in presence of approx. 5% w/v polyethylene glycol 6000 and 0.2-0.4 M MgCl2 under strictly anaerobic conditions, x-ray analysis; MoFe proteinAzotobacter vinelandii-440153
MoFe protein; purified enzyme is diluted at room temperature with 3 volumes of Tris-HCl 0.01 M, pH 7.2, immediate crystal formationAzotobacter vinelandii-440154
nitrogenase containing alpha70Ile mutant MoFe protein, 38 mg/ml protein is diluted in 50 mM Tris buffer, pH 8.0, and 250 mM NaCl, crystallization in 30% PEG 4000, 100 mM Tris, pH 8.0, 170-190 mM sodium molybdate, and 1 mM dithionite, 3-4 weeks, X-ray diffraction structure determination and analysis at 2.3 A resolution, comparison to the wild-type, with alpha70Val crystal structure, PDB ID 1M1N, overviewAzotobacter vinelandiiP07328715813
MoFe protein, crystallized in presence of approx. 5% w/v polyethylene glycol 6000 and 0.2-0.4 M MgCl2 under strictly anaerobic conditions, x-ray analysisClostridium pasteurianum-440153
purified recombinant His-tagged NifH2, hanging drop vapour diffusion method, 0.001 l of 20 mg/ml protein in 2 mM Tris-HCl, pH 8.0, and 50 mM NaCl, is mixed with 0.001 ml of reservoir solution, containing 0.1 M sodium citrate, 8% PEG 8000, pH 5.0, and equilibrated against 0.15 ml of reservoir solution, 10 days, 4C, X-ray diffraction structure determination and analysis at 2.85 A resolutionMethanocaldococcus jannaschii-713656

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
58Azotobacter chroococcum-MoFe protein stable440167
8.7-Azotobacter chroococcum-50% loss of activity after overnight dialysis at pH 8.7440167

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
22-Azotobacter vinelandii-Fe protein, half-life: 18 h440158
additional information-Azotobacter vinelandii-Fe protein: cold labile440158

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
nitrogenase complex is more stable than either the MoFe protein or the Fe protein aloneAzotobacter vinelandii-440158
Fe protein is salt sensitiveClostridium pasteurianum-440159

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
extreme sensitivity to O2Allochromatium vinosum-440142, 440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minAllochromatium vinosum-440143
extreme sensitivity to O2Anabaena cylindrica-440144
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoAnabaena sp., Anabaena variabilis-440166
stable to O2, no loss in nitrogen fixation activityAnabaena variabilis-440148
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoAzospirillum brasilense-440166
extreme sensitivity to O2Azotobacter chroococcum-440143, 440144
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoAzotobacter chroococcum-440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minAzotobacter chroococcum-440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoAzotobacter sp.-440166
extreme O2 lability, susceptibility to O2 increases with purification, but is retarded in presence of MgCl2Azotobacter vinelandii-440158
extreme sensitivity to O2Azotobacter vinelandii-440142, 440143, 440144
MoFe protein is extremely sensitive to O2Azotobacter vinelandii-440147
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoAzotobacter vinelandii-440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minAzotobacter vinelandii-440143
enzyme is extremely oxygen-labileBradyrhizobium japonicum-660287
extreme sensitivity to O2Bradyrhizobium japonicum-440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minBradyrhizobium japonicum-440143
extreme sensitivity to O2Clostridium pasteurianum-440142, 440143, 440144
Fe protein is very O2 sensitiveClostridium pasteurianum-440159
extreme sensitivity to O2Corynebacterium flavescens-440144
extreme sensitivity to O2Cyanobacterium sp.-440148
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoFrankia sp., Gloeothece sp.-440166
complete reversible inhibition by O2, reversibility decreases by increasing the time of exposure to O2, after 20 min 60% reversibility of the inhibition remainsKlebsiella pneumoniae-440140
extreme O2 lability, t1/2: 10 min, MoFe protein 45 s, Fe proteinKlebsiella pneumoniae-440149
extreme sensitivity to O2Klebsiella pneumoniae-440142, 440143, 440144
MoFe protein is extremely sensitive to O2Klebsiella pneumoniae-440147
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoKlebsiella pneumoniae-440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minKlebsiella pneumoniae-440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoOscillatoria sp.-440166
extreme sensitivity to O2Paenibacillus polymyxa-440143, 440144
extreme O2 lability, t1/2: 1 min, Fe proteinRhizobium lupini-440165
extreme sensitivity to O2Rhizobium lupini-440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minRhizobium lupini-440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivoRhizobium sp.-440166
extreme sensitivity to O2Rhodobacter capsulatus-440142
extreme sensitivity to O2Rhodospirillum rubrum-440142, 440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 minRhodospirillum rubrum-440143

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-15C, anaerobic storage, overnight, complete loss of activityAzotobacter vinelandii-440154
0C, anaerobic conditions, FeMo protein stableAzotobacter vinelandii-440158
22C, O2-free atmosphere, pH 7-8, stableAzotobacter vinelandii-440154
5C, O2-free atmosphere, overnight, 80% loss of activityAzotobacter vinelandii-440154

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Allochromatium vinosum-440143
-Anabaena cylindrica-440170
strain Y1Azospirillum amazonense-440161
-Azotobacter chroococcum-440143
large scaleAzotobacter chroococcum-440167
partially, extraction of FeVco in an active form by N-methylformamide, and gel filtration of the reconstituted protein, overviewAzotobacter chroococcum-715261
-Azotobacter vinelandii-440143, 440154, 440158, 440174, 440178
2 forms of VFe proteinAzotobacter vinelandii-440188
FeMo-cofactorless MoFe protein from nifB deletion mutantAzotobacter vinelandii-440179
large scale; strict anaerobic conditionsAzotobacter vinelandii-440163
mutant betaG69SAzotobacter vinelandiiP00459658483
recombinant Azotobacter vinelandii NafY protein from Escherichia coli strain BL21(DE3)Azotobacter vinelandii-659338
recombinant wild-type Fe protein, recombinant His-tagged wild-type MoFe protein and recombinant His-tagged MoFe protein mutant V70A, to homogeneityAzotobacter vinelandii-658010
strict anaerobic conditionsAzotobacter vinelandii-440153
wild-type and mutant H195QAzotobacter vinelandii-440184, 440189
wild-type and mutants H195Q, H195N, Q191KAzotobacter vinelandii-440181
-Clostridium pasteurianum-440143
all componentsClostridium pasteurianum-440164
strict anaerobic conditionsClostridium pasteurianum-440153, 440159
-Klebsiella pneumoniae-440143
both componentsKlebsiella pneumoniae-440157
native NifDK by gel filtration and affinity chromatography on a NifB resin, elution as NifDK/NifB-co complexKlebsiella pneumoniae-715017
purification of the enzyme complex and isolation of the MoFe protein thereofKlebsiella pneumoniae-658901
recombinant His-tagged NifH2 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration to over 95% purityMethanocaldococcus jannaschii-713656
-Paenibacillus polymyxa-440169
both componentsRhizobium lupini-440165
ORS571Rhizobium sp.-440162
-Rhodobacter capsulatus-440171
iron-only nitrogenase, both componentsRhodobacter capsulatus-440176
molybdenum containing enzyme form, both componentsRhodobacter capsulatus-440177
wild-type and tungsten-substituted enzymesRhodobacter capsulatus-657985
both componentsXanthobacter autotrophicus-440168

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinant expression of wild-type and mutant gene nifD by gene replacement, Escherichia coli strain HB101(pRL623) and J53 (RP4) are used for the transfer of mobilizable plasmids into Anabaena cells, with a deletion of nifHDK-ORF, by conjugation via triparental mating, subcloning in Escherichia coli strain XL-1 BlueAnabaena sp.-713837
amino acid sequence comparison with other species; expression in Escherichia coli, expression in Klebsiella pneumoniae, Anabaena gene library screening with genes of Klebsiella pneumoniaeAnabaena variabilis-440152
strain YM68A expresses the His-tagged VFe protein, strain YM13A expresses the His-tagged MoFe protein, and strain DJ1143 expresses the His-tagged DELTAnifB MoFe proteinAzotobacter chroococcum-715261
expression of His-tagged wild-type and V70A mutant MoFe protein in strain DJ1310, expression of the wild-type Fe proteinAzotobacter vinelandii-658010
genetic analysisAzotobacter vinelandii-440155
overexpression of Azotobacter vinelandii NafY protein in Escherichia coli strain BL21(DE3)Azotobacter vinelandii-659338
expression in Escherichia coliBradyrhizobium japonicum-440151
expression of nitrogenase in the absence of NH4+ and at initial O2 concentrations above 5% in the culture atmosphereGluconacetobacter diazotrophicus-672344
genetic mappingHerbaspirillum seropedicae-658769
phylogenetic analysis, overviewKlebsiella pneumoniae-715017
gene MJ0685, expression of His-tagged NifH2 in Escherichia coli strain BL21 (DE3)Methanocaldococcus jannaschii-713656

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
F388 AAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
F388HAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
F388TAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
F388YAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197AAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197DAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197EAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197FAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197GAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197KAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197LAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAH, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overviewup713837
H197NAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197QAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197RAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197SAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197TAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193AAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193GAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193HAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193KAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193LAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193NAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193SAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Q193VAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284CAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284EAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284FAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284HAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284KAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284LAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284QAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284TAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
R284YAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285AAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285CAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285DAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285GAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285MAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285NAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285QAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
S285TAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236AAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236DAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236FAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236HAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236MAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236NAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
Y236TAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
H197AAnabaena sp. PCC 7120-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview-
H197NAnabaena sp. PCC 7120-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview-
A175GAzotobacter vinelandii-shows in vivo 55% of enzyme activity compared to wild-type, in vitro 20% activity remaining with purified enzyme, slowlier conformational change upon binding of MgATP, model of steric interactions using x-ray crystal structures440182
A175SAzotobacter vinelandii-unable to support substrate reduction because of an inability to undergo a required MgATP-induced conformational change440182
D125EAzotobacter vinelandiiP00459site-directed mutagenesis, mutation alters the properties of the MgATP2- binding site with bound MgADP658483
G69SAzotobacter vinelandiiP00459random mutagenesis, beta-subunit residue mutant of the MoFe protein shows highly decreased affinity for acetylene, acetylene inhibits the mutants nitrogen reduction activity in a competitive mode in contrast to the wild-type enzyme658483
H195GAzotobacter vinelandii-alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, slightly decreased Fe protein activity, altered phenotype440189
H195LAzotobacter vinelandii-alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, increased Fe protein activity, altered phenotype440189
H195NAzotobacter vinelandii-alphaHis195 of MoFe protein, shows 59% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition, NH3 production decreased much less440181
H195NAzotobacter vinelandii-alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, altered phenotype440189
H195QAzotobacter vinelandii-alphaHis195 of MoFe protein, shows 159% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition440181
H195QAzotobacter vinelandii-below 2% N2 reducing activity remaining compared to wild-type due to less effective N2 binding440184
H195QAzotobacter vinelandii-alpha-His of MoFe protein, site directed mutagenesis, decreased MoFe protein activity, altered phenotype440189
H195TAzotobacter vinelandii-alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype440189
H195YAzotobacter vinelandii-alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype440189
Q191A/V70AAzotobacter vinelandii-site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene688191
Q191KAzotobacter vinelandii-alphaGln191 of MoFe protein, shows 6% activity compared to wild-type, substrate CN-, not affected by addition of C2H2440181
S188CAzotobacter vinelandiiP00459site-directed mutagenesis, mutation of a residue within the P-cluster of the beta-subunit, alters the EPR signal of the MoFe protein658483
S69GAzotobacter vinelandii-alpha-subunit MoFe protein, resistant to inhibition by C2H2, thus acetylene binding/reduction site is not directly relevant to the mechanism of nitrogen reduction440183
V70AAzotobacter vinelandii-site-directed mutagenesis of an alpha subunit residue of the MoFe cofactor, mutation alters the active site structure, trapping of propargyl alcohol at the active site for structure analysis658010
V70AAzotobacter vinelandii-site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme659426
V70AAzotobacter vinelandii-site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne688191
V70A/H195QAzotobacter vinelandii-mutant used for freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor. EPR and ENDOR analysis of the adduct672039
V70GAzotobacter vinelandii-site-directed mutagenesis, the mutant MoFe protein variant shows an increased capacity for reduction of the terminal alkyne, 1-butyne, but no detectable reduction of the internal alkyne 2-butyne688191
V70IAzotobacter vinelandii-site-directed mutagenesis, decreased the hydrazine reduction activity659426
V70IAzotobacter vinelandii-site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene688191
V70IAzotobacter vinelandii-the mutant is suitable for analysis of reaction intermediates, since it exhibits the highest concentration of trapped H+-intermediate when turned over under Ar689764
V70IAzotobacter vinelandiiP07328substitution of alpha70Val by alpha70Ile results in a MoFe protein that is hampered in its ability to reduce a range of substrates including acetylene and N2, yet retains normal proton reduction activity. The mutant shows H2 evolution of greater than 2200 nmol/min/mg MoFe protein, which is 95% of the wild-type specific activity715813
V70XAzotobacter vinelandii-site-directed mutagenesis, substitution of valine with an amino acid with a smaller side chain increases the hydrazine reduction activity, substitution with an amino acid with a larger side chain decreases the enzyme activity with N2, acetylene or hydrazine659426
H197YAnabaena sp.-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview713837
additional informationAnabaena sp.-engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview713837
H197TAnabaena sp. PCC 7120-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview-
additional informationAnabaena sp. PCC 7120-engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview-
R284QAnabaena sp. PCC 7120-site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview-
additional informationAzospirillum brasilense-reduction of nitrogenase activity in cells overexpressing PII protein participating in nif regulation is due to partial ADP-ribosylation of the Fe-protein under derepressing conditions and a reduction in the amount of Fe-protein. In cells overexpressing the PZ protein which negatively regulates ammonium transport the nitrogenase reactivation after an ammonium shock is delayed673723
K15QAzotobacter vinelandiiP00459site-directed mutagenesis, mutation inhibits the communication of the [4Fe4S] cluster with the MgATP2- binding site658483
additional informationAzotobacter vinelandii-construction of mutant strain RP114440155
additional informationAzotobacter vinelandii-natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster440179
additional informationAzotobacter vinelandii--440183
additional informationAzotobacter vinelandiiP00459deletion of nifH results in an enzyme complex with a MoFe protein exhibiting altered redox properties and no EPR signal, a Fe protein Lys127 deletion mutant mimics the MgATP-bound-conformation and inhibits nucleotide hydrolyzing activity, formation of nondissociating complex with the MoFe protein658483
additional informationAzotobacter vinelandii-study of two nifB deletion mutants, having His-tagged MoFe/VFe protein, and two nifH deletion mutants, having His-tagged MoFe proteins, with catalytically active P-cluster variants presumably composed of [4Fe-4S]-like centers that are clearly distinct from the normal P-clusters. Proteins are active in terms of H2 evolution, C2H2 reduction, and N2 fixation upon FeMoco insertion676778
additional informationAzotobacter vinelandii-construction of mutant Azotobacter vinelandii strains DJ1242, DJ1313, and DJ1495, the mutant show loss of the ability to grow under nitrogen fixing conditions, phenotypes, overview688191
additional informationAzotobacter vinelandii-in vitro synthesis of the iron-molybdenum cofactor of nitrogenase using purified proteins, a minimal in vitro system, containing NifB, NifEN, and NifH proteins, together with Fe2+, S2-, MoO4 2-, R-homocitrate, S-adenosyl methionine, and Mg-ATP, is sufficient for the synthesis of FeMo-co and the activation of apo-dinitrogenase under anaerobic-reducing conditions, modeling, overview689764
additional informationAzotobacter vinelandii-a MoFeP variant labeled on its surface with a Ru-photosensitizer is shown to photocatalytically reduce protons and acetylene, most likely at its active site, FeMoco. The uncoupling of nitrogenase catalysis from ATP hydrolysis enables the study of redox dynamics within MoFeP and the population of discrete reaction intermediates, overview715263
V70AAzotobacter vinelandii DJ1310-site-directed mutagenesis of an alpha subunit residue of the MoFe cofactor, mutation alters the active site structure, trapping of propargyl alcohol at the active site for structure analysis-
additional informationBradyrhizobium japonicum-transposon insertion mutants of several plasmids440151
additional informationHerbaspirillum seropedicae-strains mutated in the nifX or orf1 genes show 90% or 50% reduction in nitrogenase activity under low levels of iron or molybdenum, respectively658769
additional informationKlebsiella pneumoniae-generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3715017
additional informationKlebsiella pneumoniae UN1217-generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3-
additional informationRhodobacter capsulatus-construction of 2 mutants strain: 1 kanamycin-resistant with a deletion in NifHDK and 1 kanamycin, gentamycin, and molybdenum-resistant with double deletion in nif HDK and modABCD440176
additional informationRhodobacter capsulatus B10S-construction of 2 mutants strain: 1 kanamycin-resistant with a deletion in NifHDK and 1 kanamycin, gentamycin, and molybdenum-resistant with double deletion in nif HDK and modABCD-

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
native enzyme is reconstituted from N-methylformamide extractionAzotobacter chroococcum-715261
recovery of enzyme activity from aerobically isolated soybean nodules by incubation at low O2 pressure for about 1 h, recovery of activity can be inhibited by chloramphenicol and puromycin, and by spectinomycin only in strain 2134, not in strain 110, cycloheximide, actinomycin D, nalidixic acid, and rifampicin have no effect on enzyme activity recovery in strain 110, and cycloheximide, actinomycin D, and streptomycin have no effect on enzyme activity recovery in strain 2134Bradyrhizobium japonicum-660287

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
agricultureAlnus maritima-enzyme activity increases with increasing concentration of O2 in the root zone. Photosynthetic rate, plant dry mass, leaf N content, and nodule fresh mass are maximal in plants maintained with 15-25% O2 in the root zone676442
energy productionAzotobacter vinelandii-the reaction produces H2 as a by-product and is interesting for production of clean energy689764

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660287Karr, D.B.; Oehrle, N.W.; Emerich, D.W.Recovery of nitrogenase from aerobically isolated soybean nodule bacteroidsPlant Soil25727-332003Bradyrhizobium japonicum-
662028Zhang, Y.; Pohlmann, E.L.; Roberts, G.P.GlnD is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrumJ. Bacteriol.1871254-12652005Rhodospirillum rubrum PubMed
672039Barney, B.M.; Laryukhin, M.; Igarashi, R.Y.; Lee, H.I.; Dos Santos, P.C.; Yang, T.C.; Hoffman, B.M.; Dean, D.R.; Seefeldt, L.C.Trapping a hydrazine reduction intermediate on the nitrogenase active siteBiochemistry448030-80372005Azotobacter vinelandii PubMed
672344Fisher, K.; Newton, W.E.Nitrogenase proteins from Gluconacetobacter diazotrophicus, a sugarcane-colonizing bacteriumBiochim. Biophys. Acta1750154-1652005Gluconacetobacter diazotrophicus PubMed
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673723Huergo, L.F.; Filipaki, A.; Chubatsu, L.S.; Yates, M.G.; Steffens, M.B.; Pedrosa, F.O.; Souza, E.M.Effect of the over-expression of PII and PZ proteins on the nitrogenase activity of Azospirillum brasilenseFEMS Microbiol. Lett.25347-542005Azospirillum brasilense PubMed
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676049Dodsworth, J.A.; Cady, N.C.; Leigh, J.A.2-Oxoglutarate and the PII homologues NifI1 and NifI2 regulate nitrogenase activity in cell extracts of Methanococcus maripaludisMol. Microbiol.561527-15382005Methanococcus maripaludis PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 1.18.6.1)
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NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)