Information on EC 1.18.6.1 -

Information on EC 1.18.6.1 - nitrogenase:

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EC NUMBER	COMMENTARY
1.18.6.1	-

RECOMMENDED NAME	GeneOntology No.
nitrogenase	GO:0018697

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		-	-	-	-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Klebsiella 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Azotobacter 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Clostridium 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Rhodospirillum 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Paenibacillus 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Rhizobium sp.	-	440134, 440145, 440162
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Anabaena cylindrica	-	440134, 440145, 440170
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Leptolyngbya boryana	-	440134, 440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Anabaena 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		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 cycle	Azotobacter vinelandii	-	440138
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Klebsiella 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		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Azotobacter 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		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Allochromatium vinosum, Rhodospirillum rubrum	-	440142, 440144
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Rhodobacter capsulatus	-	440142
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Bradyrhizobium japonicum	-	440143, 440145, 440151
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Rhizobium lupini	-	440143, 440145, 440165
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Azotobacter 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Allochromatium vinosum	-	440143, 440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Paenibacillus polymyxa	-	440144, 440146, 440147
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Azotobacter chroococcum	-	440144, 440146
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Anabaena 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Corynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Ornithopus sativus	-	440145
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Anabaena variabilis	-	440148, 440152
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Cyanobacterium sp.	-	440148
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism	Azotobacter chroococcum	-	440150, 440166
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism; structure of V-containing enzyme form	Azotobacter vinelandii	-	440150
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Beggiatoa alba	-	440160
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Azospirillum amazonense	-	440161
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism	Anabaena sp., Anabaena variabilis, Azospirillum brasilense, Azotobacter 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Xanthobacter autotrophicus	-	440168
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Rhodobacter capsulatus	-	440171
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism	Azotobacter 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		enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; MgATP/MgADP-dependent electron and proton transfer kinetics	Azotobacter vinelandii	-	440175
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		iron-only enzyme is composed of 2 components: FeFe protein and Fe protein	Rhodobacter capsulatus	-	440176
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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	Rhodobacter capsulatus	-	440177
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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-cofactor	Azotobacter vinelandii	-	440179
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		C2H2 inhibition mechanism, structure model; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein	Azotobacter vinelandii	-	440183
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		structure of V-containing enzyme form	Azotobacter vinelandii	-	440188
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195	Azotobacter vinelandii	-	658010
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		theoretical mechanisms of substrate binding to molybdenum or iron in the FeMo cofactor, modeling	Azotobacter vinelandii	-	658040
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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, overview	Azotobacter vinelandii	P00459	658483
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		the active site is located on the MoFe protein, active site structure and substrate binding mechanism	Klebsiella pneumoniae	-	658901
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		active site location	Azotobacter vinelandii	-	659426
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		-	Bradyrhizobium japonicum	-	660287
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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 site	Azotobacter vinelandii	-	674147
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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 state	Azotobacter vinelandii	-	674154
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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 probable	Azotobacter vinelandii	-	674202
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		reaction mechanism, overview	Methanococcus maripaludis	-	684881
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate		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, overview	Azotobacter vinelandii	-	689764

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
oxidation	-	-	-	-
redox reaction	-	-	-	-
reduction	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
nitrogen fixation	-	N2FIX-PWY

SYSTEMATIC NAME

IUBMB 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)].

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
ARA	Lotus japonicus	-	-	699812
dinitrogenase	Rhodobacter capsulatus	-	-	657985
EC 1.18.2.1	-	-	formerly	-
Kp2	Klebsiella pneumoniae	-	-	687822, 687823
Mo-nitrogenase	Azotobacter chroococcum	-	-	715261
molybdenum nitrogenase	Klebsiella pneumoniae	-	-	715017
molybdenum-containing nitrogenase	Anabaena sp.	-	-	713837
NifDK	Klebsiella pneumoniae	-	-	715017
NifH2	Methanocaldococcus jannaschii	-	-	713656
nitrogenase Fe protein	Klebsiella pneumoniae	-	-	687822
nitrogenase Fe-protein	Klebsiella pneumoniae	-	-	687823
nitrogenase FeVco	Azotobacter chroococcum	-	-	715261
nitrogenase iron-protein	Klebsiella pneumoniae	-	-	687823
V-nitrogenase	Azotobacter chroococcum	-	-	715261
vanadium nitrogenase	Azotobacter vinelandii	-	-	716922
vanadium-nitrogenase	Azotobacter chroococcum	-	-	715261
molybdenum-nitrogenase	Azotobacter chroococcum	-	-	715261
additional information	Azotobacter vinelandii	-	the nitrogenase complex is composed of 2 oxygen-labile metalloproteins: dinitrogenase and dinitrogenase reductase	659338

CAS REGISTRY NUMBER	COMMENTARY
9013-04-1	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Allochromatium vinosum	-	440142, 440143, 440144, 440145	-	-
Alnus 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 zone	676442	-	-
Anabaena cylindrica	-	440134, 440144, 440145, 440170	-	-
Anabaena sp.	-	440134, 440166, 713837	-	-
Anabaena variabilis	-	440148, 440166	-	-
Anabaena variabilis	nitrogen fixation complex is encoded on nif gene cluster	440152	-	-
Azoarcus sp.	strain BH72	698619	-	-
Azoarcus sp. BH72	strain BH72	698619	-	-
Azorhizobium caulinodans ORS571	ORS571	440134	-	-
Azospirillum amazonense	strain Y1	440161	-	-
Azospirillum brasilense	-	440166, 673723	-	-
Azospirillum sp.	-	440134	-	-
Azotobacter chroococcum	-	440143, 440144, 440145, 440146, 440150, 440166, 440167	-	-
Azotobacter chroococcum	contains Mo- and V-nitrogenases	715261	-	-
Azotobacter chroococcum	nitrogen fixation complex is encoded on nif gene cluster	440186	-	-
Azotobacter chroococcum YM68A	contains Mo- and V-nitrogenases	715261	-	-
Azotobacter sp.	-	440134, 440166	-	-
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	-	-
Azotobacter vinelandii	-	658483	P00459	Uniprot
Azotobacter vinelandii	-	715813	P07328	UniProt
Azotobacter vinelandii	2 forms of VFe protein	440188	-	-
Azotobacter vinelandii	2 forms of VFe protein; nitrogen fixation complex is encoded on nif gene cluster	440186	-	-
Azotobacter vinelandii	; recombinant strain DJ1373 expressing mutant V70I	689764	-	-
Azotobacter vinelandii	contains 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 Mo	440150, 440155	-	-
Azotobacter vinelandii	contains nif-encoded molybdenum nitrogenase and vnf-encoded V nitrogenase	716922	-	-
Azotobacter vinelandii	molybdenum-dependent enzyme variant	658040	-	-
Azotobacter vinelandii	nitrogen fixation complex is encoded on nif gene cluster	440179, 440182	-	-
Azotobacter vinelandii	strain DJ	659338	-	-
Azotobacter vinelandii	strain DJ1310	658010	-	-
Azotobacter vinelandii	strain DJ995	688191	-	-
Azotobacter vinelandii	strain OP	440180	-	-
Azotobacter vinelandii	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	674202	-	-
Azotobacter vinelandii DJ1310	strain DJ1310	658010	-	-
Beggiatoa alba	strain B18LD	440160	-	-
Bradyrhizobium japonicum	-	440143, 440144	-	-
Bradyrhizobium japonicum	associated with Glycine max	440145	-	-
Bradyrhizobium japonicum	nitrogen fixation complex is encoded on nif gene cluster	440151	-	-
Bradyrhizobium japonicum	strains 110 or 2134, anaerobically and aerobically isolated bacteroid from nodules of soybean	660287	-	-
Chlorobium sp.	-	440134	-	-
Chromatium sp.	-	440134, 440174	-	-
Clostridium pasteurianum	-	440134, 440142, 440143, 440144, 440145, 440146, 440147, 440153, 440159, 440164, 440174, 440180	-	-
Clostridium pasteurianum	nitrogen fixation complex is encoded on nif gene cluster	440186	-	-
Corynebacterium flavescens	-	440144	-	-
Corynebacterium flavescens	301	440145	-	-
Corynebacterium flavescens 301	301	440145	-	-
Crocosphaera watsonii	a marine unicellular diazotrophic cyanobacterium	714845	-	-
Cyanobacterium sp.	-	440148	-	-
Desulfovibrio desulfuricans	low activity	440145	-	-
Desulfovibrio sp.	-	440134	-	-
Endomycopsis fibuligera Y1	strain Y1	440161	-	-
Escherichia coli	C-M 74	440145	-	-
Escherichia coli C-M 74	C-M 74	440145	-	-
Frankia sp.	-	440134, 440166	-	-
Gloeocapsa sp.	-	440145	-	-
Gloeothece sp.	-	440134, 440166	-	-
Gloeothece sp.	a terrestrial unicellular diazotrophic cyanobacterium	714845	-	-
Gloeothece sp. PCC6909	a terrestrial unicellular diazotrophic cyanobacterium	714845	-	-
Gluconacetobacter diazotrophicus	expression of nitrogenase in the absence of NH4+ and at initial O2 concentrations above 5% in the culture atmosphere	672344	-	-
Gluconacetobacter diazotrophicus	strain PAL-5, in endosymbiosis with sugarcane, Saccharum officinarum	658372	-	-
Gluconacetobacter diazotrophicus PAL-5	strain PAL-5, in endosymbiosis with sugarcane, Saccharum officinarum	658372	-	-
Herbaspirillum seropedicae	-	658769	-	-
Klebsiella pneumoniae	-	440134, 440140, 440142, 440143, 440144, 440145, 440146, 440149, 440157, 440166, 440174, 687822, 687823, 715017	-	-
Klebsiella pneumoniae	nitrogen fixation complex is encoded on nif gene cluster	440147, 440152	-	-
Klebsiella pneumoniae	strain M5a1	658901	-	-
Klebsiella pneumoniae UN1217	-	715017	-	-
Leptolyngbya boryana	-	440134, 440145	-	-
Lotus japonicus	inoculated with symbiont Mesorhizobium loti strain New Zealand Palmerston 2235	699812	-	-
Mesorhizobium loti	-	716483	-	-
Methanocaldococcus jannaschii	NifH2 is one of two homologues of NifH in Methanocaldococcus jannaschii	713656	-	-
Methanococcus maripaludis	-	676049, 684881	-	-
Ornithopus sativus	-	440145	-	-
Oscillatoria sp.	-	440166	-	-
Paenibacillus polymyxa	-	440134, 440143, 440144, 440145, 440146, 440147, 440169	-	-
Rhizobium leguminosarum	-	440134	-	-
Rhizobium lupini	-	440143, 440144, 440165	-	-
Rhizobium lupini	associated with Lupinus luteus	440145	-	-
Rhizobium sp.	-	440166, 440174	-	-
Rhizobium sp.	associated with Phaseolus aureus or Vigna sinensis	440145	-	-
Rhizobium sp.	ORS571	440134	-	-
Rhizobium sp.	ORS571, associated with Sesbania rostrata	440162	-	-
Rhodobacter capsulatus	-	440142, 440171	-	-
Rhodobacter capsulatus	iron-only nitrogenase and molybdenum nitrogenase; nitrogen fixation complex is encoded on nif gene cluster; strain B10S	440176, 440177	-	-
Rhodobacter capsulatus	wild-type strain B10S, molybdenum-containing, nif-encoded enzyme variant	657985	-	-
Rhodobacter capsulatus B10S	strain B10S	440176	-	-
Rhodobacter sphaeroides	-	440134	-	-
Rhodopseudomonas sp.	-	440134	-	-
Rhodospirillum rubrum	-	440134, 440142, 440143, 440144, 440145, 440166, 662028	-	-
Xanthobacter autotrophicus	-	440168	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
evolution	Azotobacter 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 cofactor	714796
evolution	Klebsiella pneumoniae	-	substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview	715017
physiological function	Anabaena sp.	-	nitrogenase, an oxygen-labile enzyme typically containing an iron-molybdenum cofactor active site, is responsible for nitrogen fixation producing photobiological H2 as a byproduct	713837
physiological function	Klebsiella 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 protein	715017
physiological function	Azotobacter vinelandii	-	the diminished H2 evolution by V nitrogenase originates from the diversion of electrons toward CO reduction, in contrast to the Mo nitrogenase	716922
evolution	Azotobacter vinelandii	-	the ability of V nitrogenase to catalyze both CO and N2 reductions suggests a potential link between the evolution of carbon and nitrogen cycles	716922
additional information	Methanocaldococcus 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 NifH	713656
additional information	Anabaena 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-cluster	713837
additional information	Azotobacter vinelandii	-	primary sequences of NifEN and MoFe proteins	714796
additional information	Crocosphaera watsonii, Gloeothece sp.	-	pattern of nitrogenase activity during the light-dark cycle, overview	714845
additional information	Azotobacter vinelandii	P07328	structure 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-cofactor	715813
additional information	Azotobacter 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 latter	716922
additional information	Azotobacter 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, overview	716924

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
(VO4)3- + ?	(VO2)+ + ?		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 vanadate	673039	-	-	?
acetylene + ?	ethylene + ?		Bradyrhizobium japonicum	-	-	660287	-	-	?
acetylene + ?	ethylene + ?		Rhodobacter capsulatus	-	-	657985	-	-	?
acetylene + ?	ethylene + ?		Klebsiella pneumoniae	-	-	658901	-	-	?
acetylene + ?	ethylene + ?		Azotobacter vinelandii	-	-	658040	-	-	?
acetylene + ?	ethylene + ?		Azotobacter vinelandii	P00459	-	658483	-	-	?
acetylene + ?	ethylene + ?		Azotobacter vinelandii	-	-	659426	-	-	?
acetylene + ?	ethylene + ?		Herbaspirillum seropedicae	-	-	658769	-	-	?
acetylene + ?	ethylene + ?		Gluconacetobacter diazotrophicus	-	-	658372	-	-	?
C2H2 + ?	?		Azotobacter vinelandii	-	-	658010	-	-	?
C2H2 + ?	H2 + ?		Gluconacetobacter diazotrophicus	-	-	672344	-	-	?
CS2 + ?	H2S + ?		Azotobacter vinelandii	P00459	slow turnover	658483	-	-	?
cyanamide + ?	?		Azotobacter vinelandii	P00459	-	658483	-	-	?
cyanide + ?	?		Azotobacter vinelandii	P00459	-	658483	-	-	?
cyanide + ?	?		Klebsiella pneumoniae	-	cyanide favors the molydenum for binding	658901	-	-	?
cyclopropene + ?	?		Klebsiella pneumoniae	-	-	658901	-	-	?
dithionite + H+ + acetylene + ATP	?		Azospirillum amazonense	-	-	440161	-	-	?
dithionite + H+ + N2 + ATP	?		Klebsiella pneumoniae	-	in vitro substrate	440140, 440157, 440174	-	-	?
dithionite + H+ + N2 + ATP	?		Clostridium pasteurianum	-	in vitro substrate	440174, 440180	-	-	?
dithionite + H+ + N2 + ATP	?		Azotobacter vinelandii	-	in vitro substrate	440138, 440150, 440156, 440174, 440175, 440180, 440187	-	-	?
dithionite + H+ + N2 + ATP	?		Anabaena cylindrica	-	in vitro substrate	440170	-	-	?
dithionite + H+ + N2 + ATP	?		Azotobacter vinelandii	-	SO2- being the actual nitrogenase reductant, reaction kinetics	440187	-	-	?
ethylene + ?	?		Rhodobacter capsulatus	-	-	657985	-	-	?
ethylene + ?	?		Klebsiella pneumoniae	-	-	658901	-	-	?
hydrazine + ?	?		Azotobacter vinelandii	-	high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme	659426	-	-	?
methyl isocyanide + ?	?		Klebsiella pneumoniae	-	-	658901	-	-	?
N2 + 8 e- + 16 ATP + 8 H+	2 NH3 + H2 + 16 ADP + 16 phosphate		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-annealing	689764	-	-	?
N2 + 8 e- + 8 H+ + 16 ATP	2 NH3 + H2 + 16 ADP + 16 phosphate		Azotobacter vinelandii	-	cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview	715263	-	-	ir
N2H4 + ?	?		Azotobacter vinelandii	P00459	-	658483	-	-	?
N2O + ?	?		Klebsiella pneumoniae	-	-	658901	-	-	?
N2O + ?	?		Azotobacter vinelandii	P00459	-	658483	-	-	?
N3- + ?	?		Klebsiella pneumoniae	-	-	658901	-	-	?
N3- + ?	?		Azotobacter vinelandii	P00459	-	658483	-	-	?
propargyl alcohol + ?	?		Azotobacter vinelandii	-	wild-type enzyme and V70A mutant MoFe protein-containing enzyme	658010	-	-	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Escherichia coli, Bradyrhizobium japonicum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhodobacter capsulatus	-	-	440142	-	440142	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhodobacter capsulatus	-	-	440176	-	440176	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhodobacter capsulatus	-	-	440177	-	440177	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Klebsiella pneumoniae	-	-	440142	-	440142	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Klebsiella pneumoniae	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Klebsiella pneumoniae	-	-	440146	-	440146	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Klebsiella pneumoniae	-	-	440157	-	440157	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Klebsiella pneumoniae	-	-	440174	-	440174	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Clostridium pasteurianum	-	-	440142	-	440142	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Clostridium pasteurianum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Clostridium pasteurianum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Clostridium pasteurianum	-	-	440174	-	440174	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Clostridium pasteurianum	-	-	440186	-	440186	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440142	-	440142	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440146	-	440146	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440154	-	440154	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440158	-	440158	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440174	-	440174	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440178	-	440178	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440181	-	440181	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440182	-	440182	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440183	-	440183	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440186	-	440186	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440187	-	440187	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440188	-	440188	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Paenibacillus polymyxa	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Paenibacillus polymyxa	-	-	440146	-	440146	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Paenibacillus polymyxa	-	-	440169	-	440169	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhodospirillum rubrum	-	-	440142	-	440142	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhodospirillum rubrum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Chromatium sp.	-	-	440174	-	440174	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhizobium sp.	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Rhizobium sp.	-	-	440174	-	440174	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Desulfovibrio desulfuricans	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Allochromatium vinosum	-	-	440142	-	440142	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Allochromatium vinosum, Rhizobium lupini, Anabaena cylindrica	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Anabaena cylindrica	-	-	440170	-	440170	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter chroococcum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter chroococcum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter chroococcum	-	-	440186	-	440186	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Leptolyngbya boryana	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Xanthobacter autotrophicus	-	-	440168	-	440168	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Gloeocapsa sp., Corynebacterium flavescens, Ornithopus sativus	-	-	440145	-	440145	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Cyanobacterium sp.	-	-	440148	-	440148	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	active site for acetylene reduction interacts not directly with N2 reduction	440183	-	-	-
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	anaerobic atmosphere	440189	reduction cycle continues until complete reduction of the substrate to ethane	440189	?
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azoarcus sp.	-	ferredoxin is the main but not the essential electron donor for nitrogenase	698619	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Azotobacter vinelandii	-	-	440184	-	440184	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Azotobacter vinelandii	-	-	440187	-	440187	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Azotobacter vinelandii	-	-	440189	-	440189	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Escherichia coli, Bradyrhizobium japonicum, Klebsiella pneumoniae	-	in absence of other acceptors	440145	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Klebsiella pneumoniae	-	in absence of other acceptors	440146	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Clostridium pasteurianum	-	in absence of other acceptors	440145, 440146	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Azotobacter vinelandii	-	in absence of other acceptors	440145, 440146, 440158	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Paenibacillus polymyxa	-	in absence of other acceptors	440145, 440146	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Rhodospirillum rubrum, Rhizobium sp., Desulfovibrio desulfuricans, Allochromatium vinosum, Rhizobium lupini, Anabaena cylindrica, Azotobacter chroococcum	-	in absence of other acceptors	440145	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Azotobacter chroococcum	-	in absence of other acceptors	440146	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		Leptolyngbya boryana, Gloeocapsa sp., Corynebacterium flavescens, Ornithopus sativus	-	in absence of other acceptors	440145	-	-	?
reduced ferredoxin + H+ + ATP	oxidized ferredoxin + H2 + ADP + phosphate		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 substrates	440176	-	440176	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Klebsiella pneumoniae	-	-	440145	-	440145	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Klebsiella pneumoniae	-	-	440174	-	-	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Clostridium pasteurianum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Clostridium pasteurianum	-	-	440174	-	-	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Azotobacter vinelandii	-	-	440145	-	440145	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Azotobacter vinelandii	-	-	440154	-	440154	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Azotobacter vinelandii	-	-	440158	-	440158	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Azotobacter vinelandii	-	-	440174	-	-	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Paenibacillus polymyxa, Rhodospirillum rubrum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Chromatium sp.	-	-	440174	-	-	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Rhizobium sp.	-	-	440145, 440174	-	-	?
reduced ferredoxin + H+ + CH3NC + ATP	oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate		Azotobacter chroococcum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440146	-	440146	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440174	-	440174	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440174	-	440174	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440186	-	440186	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440146	-	440146	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440174	-	440174	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440178	-	440178	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440181	-	440181	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440186	-	440186	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440146	-	440146	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Chromatium sp.	-	-	440174	-	440174	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440174	-	440174	-
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + CN- + ATP	oxidized ferredoxin + CH4 + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440186	-	440186	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Escherichia coli	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter sphaeroides	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	-	440151	-	440151	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter capsulatus	-	-	440142	-	440142	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter capsulatus	-	-	440171	-	440171	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter capsulatus	-	-	440176	-	440176	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter capsulatus	-	-	440177	-	440177	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440140	-	440140	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440142	-	440142	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440147	-	440147	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440149	-	440149	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440152	-	440152	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440157	-	440157	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440142	-	440142	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440147	-	440147	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440153	-	440153	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440159	-	440159	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440164	-	440164	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440180	-	440180	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440138, 440142	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440142	-	440142	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440147	-	440147	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440150	-	440150	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440153	-	440153	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440154, 440155	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440155	-	440155	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440156	-	440156	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440158	-	440158	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440163	-	440163	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440175, 440178	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440178	-	440178	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440179	-	440179	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440180	-	440180	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440181	-	440181	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440182, 440183	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440183	-	440183	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440184	-	440184	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440187	-	440187	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440188	-	440188	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440189	-	440189	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440147	-	440147	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440169	-	440169	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azospirillum brasilense	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440142	-	440142	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Chromatium sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Chromatium sp.	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440162	-	440162	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium leguminosarum	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Desulfovibrio desulfuricans	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodopseudomonas sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Allochromatium vinosum	-	-	440142	-	440142	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Allochromatium vinosum	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Allochromatium vinosum	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Allochromatium vinosum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena variabilis	-	-	440148	-	440148	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena variabilis	-	-	440152	-	440152	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena variabilis	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Desulfovibrio sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium lupini	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium lupini	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium lupini	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium lupini	-	-	440165	-	440165	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena sp.	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena cylindrica	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena cylindrica	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena cylindrica	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena cylindrica	-	-	440170	-	440170	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azospirillum amazonense	-	-	440161	-	440161	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Frankia sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Frankia sp.	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440143	-	440143	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440150	-	440150	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440167	-	440167	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Leptolyngbya boryana	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Leptolyngbya boryana	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter sp.	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Xanthobacter autotrophicus	-	-	440168	-	440168	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Gloeocapsa sp.	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Chlorobium sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Oscillatoria sp.	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Corynebacterium flavescens	-	-	440144	-	440144	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Corynebacterium flavescens	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Ornithopus sativus	-	-	440145	-	440145	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Cyanobacterium sp.	-	-	440148	-	440148	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Beggiatoa alba	-	-	440160	-	440160	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azospirillum sp., Gloeothece sp.	-	-	440134	-	440134	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Gloeothece sp.	-	-	440166	-	440166	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	slow enzyme	440138	-	440138	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	1-propyne, 1-butyne and allene are reduced to the corresponding alkenes	440154	-	440154	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		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 cycle	440138	-	440138	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	MgATP-dependent	440186	-	440186	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	MgATP-dependent	440175	-	440175	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	MgATP-dependent	440182	-	440182	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii, Azotobacter chroococcum	-	MgATP-dependent	440186	-	440186	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Cyanobacterium sp.	-	ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin, regulation	440148	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter sphaeroides, Klebsiella pneumoniae, Clostridium pasteurianum	-	biological N2 fixation	440134	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	biological N2 fixation	440186	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	biological N2 fixation	440134, 440186	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	biological N2 fixation	440188	-	440188	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa, Rhodospirillum rubrum, Chromatium sp., Rhizobium sp., Rhizobium leguminosarum, Rhodopseudomonas sp., Desulfovibrio sp., Anabaena sp., Anabaena cylindrica, Frankia sp.	-	biological N2 fixation	440134	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	biological N2 fixation	440186	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Leptolyngbya boryana, Azotobacter sp., Chlorobium sp.	-	biological N2 fixation	440134	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Cyanobacterium sp.	-	biological N2 fixation	440148	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Gloeothece sp.	-	biological N2 fixation	440134	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		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 nitrogenase	440134	-	-	?
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	687822, 687823	-	-	?
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	-	660287	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	658901	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	658010, 659426	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Herbaspirillum seropedicae	-	-	658769	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Methanococcus maripaludis	-	-	684881	-	-	?
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Gluconacetobacter diazotrophicus	-	-	658372	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	biological nitrogen fixation	658040	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Gluconacetobacter diazotrophicus	-	biological nitrogen fixation	658372	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	P00459	enzyme complex is responsible for the majority of biological nitrogen fixation	658483	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	reduction of atmospheric dinitrogen to ammonium	660287	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	in absence of N2 or other substrates, the electron flow is directed towards proton reduction	658040	-	-	ir
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	P00459	turnover 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 protein	658483	-	-	ir
reduced ferredoxin + H+ + N2O + ATP	oxidized ferredoxin + H2O + N2 + ADP + phosphate		Klebsiella pneumoniae, Clostridium pasteurianum, Azotobacter vinelandii, Paenibacillus polymyxa, Azotobacter chroococcum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Klebsiella pneumoniae	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Klebsiella pneumoniae	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Clostridium pasteurianum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Clostridium pasteurianum	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Clostridium pasteurianum	-	-	440186	-	440186	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	-	440154	-	440154	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	-	440158	-	440158	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	-	440178	-	440178	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	-	440186	-	440186	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Paenibacillus polymyxa	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Chromatium sp., Rhizobium sp.	-	-	440174	-	440174	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter chroococcum	-	-	440146	-	440146	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter chroococcum	-	-	440186	-	440186	?
reduced ferredoxin + H+ + N3- + ATP	oxidized ferredoxin + NH3 + N2 + ADP + phosphate		Azotobacter vinelandii	-	mutant H195Q shows only about 7.5% activity compared to wild-type	440184	-	440184	?
reduced ferredoxin + H+ + SCN- + ATP	oxidized ferredoxin + H2S + HCN + ADP + phosphate		Azotobacter vinelandii	-	-	440178	-	440178	?
reduced flavodoxin + H+ + N2 + ATP	oxidized flavodoxin + NH3 + ADP + phosphate		Rhodobacter capsulatus, Klebsiella pneumoniae, Clostridium pasteurianum, Azotobacter vinelandii	-	-	440142	-	-	?
reduced flavodoxin + H+ + N2 + ATP	oxidized flavodoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440150	-	-	?
reduced flavodoxin + H+ + N2 + ATP	oxidized flavodoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum, Allochromatium vinosum	-	-	440142	-	-	?
reduced flavodoxin + H+ + N2 + ATP	oxidized flavodoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	intermediate is a flavodoxin hydroquinone	440138	-	440138	?
Ti3+ + H+ + N2 + ATP	?		Clostridium pasteurianum, Azotobacter vinelandii	-	in vitro substrate	440180	-	-	?
methyl isocyanide + ?	?		Azotobacter vinelandii	P00459	-	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 clusters	658769	-	-	-
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, overview	658372	-	-	-
additional information	?	-	Azotobacter vinelandii	P00459	the 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 protein	658483	-	-	-
additional information	?	-	Methanococcus maripaludis	-	both nifI1 and nifI2 are required for regulation in vivo	684881	-	-	-
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, overview	688191	-	-	-
additional information	?	-	Methanococcus maripaludis	-	the enzyme performs acetylene reduction	684881	-	-	-
additional information	?	-	Mesorhizobium loti	-	enzyme activity causes acetylene production	716483	-	-	-
additional information	?	-	Azotobacter vinelandii	-	nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor	714796	-	-	-
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 NH3	715261	-	-	-
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 NH3	715017	-	-	-
additional information	?	-	Azotobacter vinelandii	P07328	substrates 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 blocked	715813	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
N2 + 8 e- + 16 ATP + 8 H+	2 NH3 + H2 + 16 ADP + 16 phosphate		Azotobacter vinelandii	-	the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3	689764	-	-
N2 + 8 e- + 8 H+ + 16 ATP	2 NH3 + H2 + 16 ADP + 16 phosphate		Azotobacter vinelandii	-	-	715263	-	-
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Azotobacter vinelandii	-	-	440183	-	440183
reduced ferredoxin + H+ + acetylene + ATP	oxidized ferredoxin + ethylene + ADP + phosphate		Anabaena cylindrica	-	-	440170	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Escherichia coli	-	-	440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	-	440143, 440144, 440145, 440151	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter capsulatus	-	-	440142, 440171, 440176, 440177	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440140, 440142, 440143, 440144, 440145, 440146, 440147, 440149, 440152, 440157, 440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	440174	-	440174
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	-	440142, 440143, 440144, 440145, 440146, 440147, 440153, 440159, 440164, 440174, 440180	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440138, 440142, 440143, 440144, 440145, 440146, 440147, 440150, 440153, 440154, 440155, 440156, 440158, 440163, 440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440174	-	440174
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	440175, 440178, 440179, 440180, 440181, 440182, 440183, 440184, 440187	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa	-	-	440143, 440144, 440145, 440146, 440147, 440169	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azospirillum brasilense	-	-	440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodospirillum rubrum	-	-	440142, 440143, 440144, 440145, 440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Chromatium sp.	-	-	440174	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium sp.	-	-	440145, 440162, 440166, 440174	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Desulfovibrio desulfuricans	-	-	440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Allochromatium vinosum	-	-	440142, 440143, 440144, 440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena variabilis	-	-	440148, 440152, 440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhizobium lupini	-	-	440143, 440144, 440145, 440165	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena sp.	-	-	440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Anabaena cylindrica	-	-	440144, 440145, 440170	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azospirillum amazonense	-	-	440161	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Frankia sp.	-	-	440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	-	440143, 440144, 440145, 440146, 440150, 440166, 440167	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Leptolyngbya boryana	-	-	440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter sp.	-	-	440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Xanthobacter autotrophicus	-	-	440168	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Gloeocapsa sp.	-	-	440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Oscillatoria sp.	-	-	440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Corynebacterium flavescens	-	-	440144, 440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Ornithopus sativus	-	-	440145	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Beggiatoa alba	-	-	440160	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azospirillum sp.	-	-	440134	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Gloeothece sp.	-	-	440166	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Cyanobacterium sp.	-	ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin, regulation	440148	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Rhodobacter sphaeroides, Klebsiella pneumoniae, Clostridium pasteurianum	-	biological N2 fixation	440134	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Clostridium pasteurianum	-	biological N2 fixation	440186	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	biological N2 fixation	440134, 440186	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter vinelandii	-	biological N2 fixation	440188	-	440188
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Paenibacillus polymyxa, Rhodospirillum rubrum, Chromatium sp., Rhizobium sp., Rhizobium leguminosarum, Rhodopseudomonas sp., Desulfovibrio sp., Anabaena sp., Anabaena cylindrica, Frankia sp.	-	biological N2 fixation	440134	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Azotobacter chroococcum	-	biological N2 fixation	440186	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Leptolyngbya boryana, Azotobacter sp., Chlorobium sp.	-	biological N2 fixation	440134	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Cyanobacterium sp.	-	biological N2 fixation	440148	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		Gloeothece sp.	-	biological N2 fixation	440134	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + NH3 + ADP + phosphate		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 nitrogenase	440134	-	-
reduced ferredoxin + H+ + N2 + ATP	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	687822, 687823	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Klebsiella pneumoniae	-	-	658901	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	-	658010, 659426	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Herbaspirillum seropedicae	-	-	658769	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Methanococcus maripaludis	-	-	684881	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	-	biological nitrogen fixation	658040	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Gluconacetobacter diazotrophicus	-	biological nitrogen fixation	658372	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Azotobacter vinelandii	P00459	enzyme complex is responsible for the majority of biological nitrogen fixation	658483	-	-
reduced ferredoxin + H+ + N2 + ATP + H2O	oxidized ferredoxin + H2 + NH3 + ADP + phosphate		Bradyrhizobium japonicum	-	reduction of atmospheric dinitrogen to ammonium	660287	-	-
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 clusters	658769	-	-
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, overview	658372	-	-
additional information	?	-	Azotobacter vinelandii	P00459	the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview	658483	-	-
additional information	?	-	Methanococcus maripaludis	-	both nifI1 and nifI2 are required for regulation in vivo	684881	-	-
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	688191	-	-
additional information	?	-	Mesorhizobium loti	-	enzyme activity causes acetylene production	716483	-	-
additional information	?	-	Azotobacter vinelandii	-	nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor	714796	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Azotobacter vinelandii	-	-	658040, 688191, 689764, 715263, 716922	2D-image
ATP	Gluconacetobacter diazotrophicus	-	-	658372	2D-image
ATP	Azotobacter vinelandii	P00459	2 MgATP binding sites on the iron protein, binding changes the redox status of the [4Fe4S] cluster of the iron protein, mechanism, overview	658483	2D-image
ATP	Herbaspirillum seropedicae	-	-	658769	2D-image
ATP	Klebsiella pneumoniae	-	-	658901, 687823, 715017	2D-image
ATP	Bradyrhizobium japonicum	-	-	660287	2D-image
ATP	Methanococcus maripaludis	-	-	684881	2D-image
ATP	Klebsiella pneumoniae	-	the FeS cluster exhibits very little change upon MgATP binding	687822	2D-image
ATP	Azoarcus sp.	-	-	698619	2D-image
ATP	Anabaena sp.	-	the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein	713837	2D-image
FeMo cofactor	Methanococcus maripaludis	-	-	684881	2D-image
FeMo cofactor	Azotobacter vinelandii	-	structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein	688191	2D-image
FeMo cofactor	Anabaena 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-cluster	713837	2D-image
FeMo cofactor	Azotobacter chroococcum	-	i.e. FeMoco cofactor, in the Mo-nitrogenase	715261	2D-image
FeMo cofactor	Azotobacter vinelandii	-	binding structure and mechanism, overview	715263	2D-image
FeMo cofactor	Azotobacter 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, overview	716924	2D-image
FeMo protein	Azotobacter 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, overview	688191	-
FeMo protein	Azotobacter 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, overview	689764	-
Ferredoxin	Azotobacter vinelandii	-	-	658010, 658040, 658483, 659426	-
Ferredoxin	Gluconacetobacter diazotrophicus	-	-	658372	-
Ferredoxin	Herbaspirillum seropedicae	-	-	658769	-
Ferredoxin	Klebsiella pneumoniae	-	-	658901	-
Ferredoxin	Bradyrhizobium japonicum	-	-	660287	-
iron cofactor	Anabaena sp.	-	the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein	713837	-
iron-molybdenum cofactor	Rhodobacter capsulatus	-	-	657985	2D-image
iron-molybdenum cofactor	Azotobacter 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 analysis	658010	2D-image
iron-molybdenum cofactor	Azotobacter vinelandii	-	enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, structure, redox status, part of the MoFe protein	658040	2D-image
iron-molybdenum cofactor	Klebsiella pneumoniae	-	-	658901	2D-image
iron-molybdenum cofactor	Azotobacter 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 sites	659338	2D-image
iron-molybdenum cofactor	Azotobacter vinelandii	-	substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis	659426	2D-image
iron-molybdenum cofactor	Azotobacter 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 protein	714796	2D-image
iron-molybdenum cofactor	Klebsiella pneumoniae	-	located at the active site in the MoFe protein	715017	2D-image
iron-molybdenum cofactor	Azotobacter vinelandii	P07328	modelling of the FeMo-cofactor binding site in the alpha70Ile MoFe protein structure	715813	2D-image
iron-vanadium cofactor	Azotobacter chroococcum	-	i.e. FeVco cofactor, in the V-nitrogenase	715261	-
MgATP2-	Azotobacter vinelandii	-	required	714796	2D-image
additional information	Azotobacter 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 transfer	440186	-
additional information	Azotobacter vinelandii	-	structure of MoFe-cofactor	440189	-
additional information	Azotobacter 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, overview	714796	-
additional information	Azotobacter 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, overview	715261	-

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ca2+	Klebsiella pneumoniae	-	1.2 gatom per mol of MoFe protein	440149
Co2+	Azotobacter vinelandii	-	divalent cation requirement is satisfied by Co2+, is best supported by concentrations of divalent cation one-half the concentration of ATP	440154
Co2+	Azotobacter vinelandii	-	can replace Mg2+, but is less effective	440158
Cu2+	Klebsiella pneumoniae	-	1.4 gatom per mol of MoFe protein	440149
Fe	Azotobacter 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, overview	714796
Fe	Klebsiella pneumoniae	-	in the active site iron-molybdenum cofactor, and as 4Fe-4S cluster in the Fe protein	715017
Fe2+	Azotobacter vinelandii	-	divalent cation requirement is satisfied by Fe2+, is best supported by concentrations of divalent cation one-half the concentration of ATP	440154
Fe2+	Azotobacter vinelandii	-	can replace Mg2+, but is less effective	440158
Fe2+	Methanococcus maripaludis	-	as part of the Fe protein in the MoFe protein, [4Fe-4S] clusters	684881
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 protein	687822
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, overview	687823
Fe2+	Azotobacter vinelandii	-	in [Fe-S] clusters	688191
Fe2+	Azotobacter vinelandii	-	part of the iron-molybdenum and molybdenum-iron cofactors	689764
Fe2+	Anabaena sp.	-	-	713837
Iron	Azotobacter vinelandii	-	-	440134, 440138, 440146, 440158, 440166, 440174, 440175, 440181, 440182
Iron	Clostridium pasteurianum	-	-	440134, 440142, 440146, 440147, 440159, 440174
Iron	Paenibacillus polymyxa	-	-	440134, 440143, 440146, 440147, 440169
Iron	Rhodospirillum rubrum	-	-	440134, 440143, 440166
Iron	Klebsiella pneumoniae	-	-	440134, 440146, 440157, 440166, 440174
Iron	Rhizobium sp.	-	-	440134, 440166, 440174
Iron	Anabaena sp., Azotobacter sp., Frankia sp., Gloeothece sp.	-	-	440134, 440166
Iron	Anabaena cylindrica	-	-	440134, 440170
Iron	Chromatium sp.	-	-	440134, 440174
Iron	Azospirillum sp., Chlorobium sp., Desulfovibrio sp., Leptolyngbya boryana, Rhizobium leguminosarum, Rhodobacter sphaeroides, Rhodopseudomonas sp.	-	-	440134
Iron	Allochromatium 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 complex	440142
Iron	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 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 MoFe6S8-9	440142
Iron	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 complex	440142
Iron	Rhodobacter 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 complex	440142
Iron	Rhodospirillum 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 complex	440142
Iron	Azotobacter chroococcum	-	-	440143, 440146, 440166
Iron	Allochromatium vinosum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae	-	17-19 atoms of iron per molecule of MoFe protein, overview	440143
Iron	Rhizobium lupini	-	-	440143
Iron	Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens	-	18-36 atoms of iron per molecule of MoFe protein , overview	440145
Iron	Desulfovibrio desulfuricans	-	18-36 atoms of iron per molecule of MoFe protein , overview; iron content of the iron protein: 3.5	440145
Iron	Escherichia 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 , overview	440145
Iron	Azotobacter 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 complex	440147
Iron	Klebsiella pneumoniae	-	17.5 gatom per mol of MoFe protein; 4 atoms of iron per molecule of Fe protein	440149
Iron	Azotobacter vinelandii	-	characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins	440156
Iron	Azospirillum amazonense	-	24 atoms of iron per molecule of MoFe protein	440161
Iron	Rhizobium sp.	-	22.5 atoms of iron per molecule of protein; 3.1	440162
Iron	Rhizobium lupini	-	4 atoms of iron per molecule of Fe protein	440165
Iron	Anabaena variabilis, Azospirillum brasilense, Oscillatoria sp.	-	-	440166
Iron	Azotobacter chroococcum	-	4 atoms of iron per molecule of Fe protein	440167
Iron	Xanthobacter autotrophicus	-	-	440168
Iron	Rhodobacter capsulatus	-	-	440171
Iron	Rhodobacter capsulatus	-	the iron-only enzyme consists of 2 components: Fe protein and FeFe protein, the latter contains 26 Fe atoms per molecul of protein	440176
Iron	Azotobacter vinelandii	-	contains [4Fe4S] cluster	440179, 440183, 440186
Iron	Azotobacter vinelandii, Clostridium pasteurianum	-	contains [4Fe4S] cluster; reduction kinetics	440180
Iron	Azotobacter chroococcum, Clostridium pasteurianum	-	contains [4Fe4S] cluster	440186
Iron	Azotobacter 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 cluster	440188
Iron	Rhodobacter capsulatus	-	required, part of the MoFe protein cofactor	657985
Iron	Azotobacter vinelandii	-	dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the enzyme complex contains also a dimeric iron protein	658010
Iron	Azotobacter 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 binding	658040
Iron	Azotobacter vinelandii	P00459	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 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, overview	658483
Iron	Herbaspirillum 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 gene	658769
Iron	Klebsiella pneumoniae	-	dependent on, the enzyme complex contains a molybdenum-iron protein, and a dimeric iron protein	658901
Iron	Azotobacter vinelandii	-	enzyme contains an iron-molybdenum cofactor	659338
Iron	Azotobacter 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-cofactor	672039
Iron	Gluconacetobacter diazotrophicus	-	component Gd1, iron and molybdenum in a 12:1 ratio. Component Gd2, 3.9 Fe atoms per molecule	672344
Iron	Azotobacter vinelandii	P07328	in FeMo cofactor and MoFe protein	715813
Iron	Azotobacter vinelandii	-	in the MoFe protein and the Fe protein	716922
Iron	Azotobacter vinelandii	-	in the FeMo cofactor	716924
Mg2+	Azotobacter vinelandii	-	-	440134, 658010, 659426, 688191, 689764
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+	Azotobacter vinelandii	-	Mg2+ required for MgATP complex	440138, 440144, 440145, 440146, 440147, 440158, 440166, 440174, 440175, 440178, 440180, 440182, 440184, 440186, 440187
Mg2+	Klebsiella pneumoniae	-	Mg2+ required for MgATP complex	440144, 440145, 440146, 440147, 440157, 440166, 440174
Mg2+	Clostridium pasteurianum	-	Mg2+ required for MgATP complex	440144, 440145, 440146, 440147, 440164, 440174, 440180, 440186
Mg2+	Paenibacillus polymyxa	-	Mg2+ required for MgATP complex	440144, 440145, 440146, 440147
Mg2+	Azotobacter chroococcum	-	Mg2+ required for MgATP complex	440144, 440145, 440146, 440166, 440186
Mg2+	Rhodospirillum rubrum	-	Mg2+ required for MgATP complex	440144, 440145, 440166
Mg2+	Allochromatium vinosum, Anabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens, Rhizobium lupini	-	Mg2+ required for MgATP complex	440144, 440145
Mg2+	Rhizobium sp.	-	Mg2+ required for MgATP complex	440145, 440166, 440174
Mg2+	Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus	-	Mg2+ required for MgATP complex	440145
Mg2+	Klebsiella pneumoniae	-	1.8 gatom per mol of MoFe protein; Mg2+ required for MgATP complex	440149
Mg2+	Azotobacter vinelandii	-	divalent metal requirement is satisfied by Mg2+, reaction is best supported by concentration of divalent cation one-half the concentration of ATP	440154
Mg2+	Anabaena sp., Anabaena variabilis, Azospirillum brasilense, Azotobacter sp., Frankia sp., Gloeothece sp., Oscillatoria sp.	-	Mg2+ required for MgATP complex	440166
Mg2+	Chromatium sp.	-	Mg2+ required for MgATP complex	440174
Mg2+	Azotobacter vinelandii	P00459	required 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, overview	658483
Mg2+	Klebsiella pneumoniae	-	required, the FeS cluster exhibits very little change upon MgATP binding	687822
Mg2+	Azotobacter vinelandii	-	MgATP2- is required	714796
Mg2+	Azotobacter vinelandii	-	required	715263
Mn2+	Azotobacter vinelandii	-	divalent cation requirement is satisfied by Mn2+, is best supported by concentrations of divalent cation one-half the concentration of ATP	440154
Mn2+	Azotobacter vinelandii	-	can replace Mg2+, but is less effective	440158
Mo	Azotobacter 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-subunit	714796
Mo	Klebsiella pneumoniae	-	in the active site iron-molybdenum cofactor	715017
Molybdenum	Azotobacter vinelandii	-	-	440134, 440138, 440158, 440166, 440175, 440179, 440182, 440183
Molybdenum	Clostridium pasteurianum	-	-	440134, 440142, 440159
Molybdenum	Klebsiella pneumoniae	-	-	440134, 440157, 440166
Molybdenum	Anabaena sp.	-	-	440134, 440166, 713837
Molybdenum	Azotobacter sp., Frankia sp., Gloeothece sp., Rhizobium sp., Rhodospirillum rubrum	-	-	440134, 440166
Molybdenum	Paenibacillus polymyxa	-	-	440134, 440169
Molybdenum	Anabaena cylindrica	-	-	440134, 440170
Molybdenum	Azospirillum sp., Chlorobium sp., Chromatium sp., Desulfovibrio sp., Leptolyngbya boryana, Rhizobium leguminosarum, Rhodobacter sphaeroides, Rhodopseudomonas sp.	-	-	440134
Molybdenum	Allochromatium 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 complex	440142
Molybdenum	Azotobacter 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 complex	440142
Molybdenum	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 complex	440142
Molybdenum	Rhodobacter 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 complex	440142
Molybdenum	Rhodospirillum 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 complex	440142
Molybdenum	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	-	1-2 gatom per mol of MoFe protein , overview	440143, 440145, 440146
Molybdenum	Allochromatium vinosum, Bradyrhizobium japonicum, Rhizobium lupini, Rhodospirillum rubrum	-	1-2 gatom per mol of MoFe protein , overview	440143, 440145
Molybdenum	Anabaena cylindrica, Corynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus, Rhizobium sp.	-	1-2 gatom per mol of MoFe protein , overview	440145
Molybdenum	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 complex; molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview; review on molybdenum in nitrogenase	440147
Molybdenum	Clostridium pasteurianum	-	molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview; review on molybdenum in nitrogenase	440147
Molybdenum	Klebsiella 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 nitrogenase	440147
Molybdenum	Paenibacillus polymyxa	-	review on molybdenum in nitrogenase	440147
Molybdenum	Anabaena variabilis	-	-	440148, 440166
Molybdenum	Cyanobacterium 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 complex	440148
Molybdenum	Klebsiella pneumoniae	-	1 gatom per mol of MoFe protein	440149
Molybdenum	Azotobacter vinelandii	-	also possesses Mo-independent nitrogenases: one vanadium containing nitrogenase and another lacking both molybdenum and vanadium	440150, 440155
Molybdenum	Azotobacter chroococcum	-	-	440150, 440166
Molybdenum	Azotobacter vinelandii	-	characterization of the metal clusters in the nitrogenase molybdenum-iron protein	440156
Molybdenum	Azospirillum amazonense	-	2 gatom per mol of MoFe protein	440161
Molybdenum	Rhizobium sp.	-	1.2-1.3 gatom per mol of MoFe protein	440162
Molybdenum	Rhizobium lupini	-	-	440165
Molybdenum	Azospirillum brasilense, Oscillatoria sp.	-	-	440166
Molybdenum	Azotobacter chroococcum	-	23 mol Fe + 1.9 mol Mo per mol of MoFe protein	440167
Molybdenum	Xanthobacter autotrophicus	-	-	440168
Molybdenum	Rhodobacter capsulatus	-	-	440171
Molybdenum	Azotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.	-	molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview	440174
Molybdenum	Azotobacter vinelandii	-	mol Mo per mol MoFeprotein: wild-type and mutant H195Q 1.9, mutant H195N and Q191K 0.9	440181
Molybdenum	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum	-	MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands	440186
Molybdenum	Rhodobacter 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 rhenium	657985
Molybdenum	Azotobacter 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 analysis	658010
Molybdenum	Azotobacter 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 site	658040
Molybdenum	Azotobacter vinelandii	P00459	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 [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, overview	658483
Molybdenum	Herbaspirillum 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	658769
Molybdenum	Klebsiella pneumoniae	-	dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site	658901
Molybdenum	Azotobacter vinelandii	-	enzyme contains an iron-molybdenum cofactor	659338
Molybdenum	Azotobacter 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-cofactor	672039
Molybdenum	Gluconacetobacter diazotrophicus	-	component Gd1, iron and molybdenum in a 12:1 ratio, molybdenum content is 1.4 atoms per enzyme tetramer	672344
Molybdenum	Azotobacter vinelandii	-	part of the iron-molybdenum and molybdenum-iron cofactors	689764
Molybdenum	Azotobacter chroococcum	-	in the FeMoco cofactor of the MoFe protein	715261
Molybdenum	Azotobacter vinelandii	P07328	in FeMo cofactor and MoFe protein	715813
Molybdenum	Azotobacter vinelandii	-	in the MoFe protein	716922
Ni2+	Azotobacter vinelandii	-	divalent cation requirement is satisfied by Ni2+, is best supported by concentrations of divalent cation one-half the concentration of ATP	440154
Ni2+	Azotobacter vinelandii	-	can replace Mg2+, but is less effective	440158
Tungsten	Rhodobacter 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 medium	657985
Vanadium	Azotobacter vinelandii	-	possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium	440150, 440155
Vanadium	Azotobacter chroococcum	-	possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium	440150
Vanadium	Azotobacter vinelandii	-	characterization of the metal clusters in the nitrogenase vanadium-iron protein	440156, 440186
Vanadium	Azotobacter chroococcum, Clostridium pasteurianum	-	characterization of the metal clusters in the nitrogenase vanadium-iron protein	440186
Vanadium	Azotobacter 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 cluster	440188
Vanadium	Azotobacter chroococcum	-	in the FeVco cofactor	715261
Zn2+	Klebsiella pneumoniae	-	0.8 gatom per mol of MoFe protein	440149
Molybdenum	Azotobacter vinelandii	-	in the FeMo cofactor	716924
additional information	Anabaena 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 information	Allochromatium 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 metals	440144
additional information	Azotobacter vinelandii	-	-	440150, 440174
additional information	Azotobacter chroococcum	-	-	440150
additional information	Chromatium sp.	-	-	440174
additional information	Clostridium pasteurianum	-	contains also an inactive MoFe protein species	440174
additional information	Klebsiella pneumoniae, Rhizobium sp.	-	-	440174
additional information	Rhodobacter capsulatus	-	the iron-only nitrogenase form contains no molybdenum, vanadium or any other heterometal atom	440176
additional information	Rhodobacter capsulatus	-	redox properties of metal clusters	440177
additional information	Azotobacter vinelandii	-	structure and organization of metal clusters	440186, 440188, 440189
additional information	Azotobacter chroococcum, Clostridium pasteurianum	-	structure and organization of metal clusters	440186
additional information	Rhodobacter capsulatus	-	rhenium cannot substitute for molybdenum in vitro, nor in vivo	657985
additional information	Azotobacter vinelandii	P00459	structure catalytic role, and mechanism of the P-cluster, part of the MoFe protein, which has a role in immediate electron acceptance from the Fe protein	658483
additional information	Azotobacter vinelandii	-	structures of the metal centers in Fe protein and MoFe protein, overview	714796

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
1,10-phenanthroline	Azotobacter vinelandii	-	-	440154	2D-image
1,2-Dihydroxybenzene 3,5-disulfonate	Azotobacter vinelandii	-	-	440154	2D-image
2,2'-dipyridyl	Azotobacter vinelandii	-	-	440154	2D-image
2,3-Dimercaptopropanol	Azotobacter vinelandii	-	-	440154	2D-image
Acetylene	Azotobacter vinelandii	-	noncompetitive inhibition of N2 reduction	658040	2D-image
Acetylene	Azotobacter vinelandii	P00459	noncompetitive inhibition of nitrogen reduction, Gly69 is important	658483	2D-image
ADP	Azotobacter vinelandii	-	-	440154	2D-image
ADP	Azotobacter vinelandii	-	above 5 mM	440158	2D-image
ATP	Azotobacter vinelandii	-	-	440158	2D-image
beryllium fluoride	Azotobacter vinelandii	P00459	inhibits by trapping of a stable Fe protein-MoFe protein nitrogenase complex	658483	2D-image
C2H2	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	-	noncompetitive inhibitor of N2 reduction	440146	2D-image
C2H2	Azotobacter vinelandii	-	inhibition of H195 mutants	440180	2D-image
C2H2	Clostridium pasteurianum	-	-	440180	2D-image
C2H2	Azotobacter vinelandii	-	competitive to N2	440183	2D-image
Ca2+	Azotobacter vinelandii	-	-	440158	2D-image
CO	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	-	noncompetitive inhibitor of N2, C2H2 and N3- reduction, no inhibition of H+ reduction	440146	2D-image
CO	Azotobacter vinelandii	-	-	440147, 440154, 440158, 440183, 658040	2D-image
CO	Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	-	-	440147	2D-image
CO	Azotobacter vinelandii	-	inhibition of CH4 and NH3 production from CN-	440181	2D-image
CO	Azotobacter vinelandii	-	inhibition of H+ reduction by about 50%	440189	2D-image
CO	Azotobacter vinelandii	-	binds to the active site	658010	2D-image
CO	Azotobacter vinelandii	P00459	strong inhibition, binding site and inhibition mechanism	658483	2D-image
Cu2+	Azotobacter vinelandii	-	-	440154	2D-image
cyanide	Azotobacter vinelandii	P00459	-	658483	2D-image
cyanide	Klebsiella pneumoniae	-	inhibits electron flow	658901	2D-image
glutamine	Rhodobacter capsulatus, Rhodospirillum rubrum	-	-	440142	2D-image
H2	Klebsiella pneumoniae, Paenibacillus polymyxa	-	-	440144, 440146	2D-image
H2	Azotobacter vinelandii	-	-	440144, 440154, 440158	2D-image
H2	Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Rhizobium lupini, Rhodospirillum rubrum	-	-	440144	2D-image
H2	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum	-	competitive inhibitor of N2, no inhibition of N3-, C2H2, CN- or H+ reduction	440146	2D-image
H2	Azotobacter vinelandii	-	competitive	440183	2D-image
H2	Azotobacter vinelandii	-	competitive inhibition of N2 binding	658040	2D-image
hydrazine	Azotobacter vinelandii	-	and derivatives	440158	2D-image
L-asparagine	Gluconacetobacter diazotrophicus	-	76% inhibition at 10 mM asparagine in the growth medium	658372	2D-image
L-aspartic acid	Gluconacetobacter diazotrophicus	-	67% inhibition at 10 mM aspartic acid in the growth medium	658372	2D-image
L-cysteine	Gluconacetobacter diazotrophicus	-	51% inhibition at 5 mM cysteine in the growth medium	658372	2D-image
L-Glutamic acid	Gluconacetobacter diazotrophicus	-	68% inhibition at 10 mM glutamic acid in the growth medium	658372	2D-image
L-glutamine	Gluconacetobacter diazotrophicus	-	60% inhibition at 10 mM glutamine in the growth medium	658372	2D-image
L-leucine	Gluconacetobacter diazotrophicus	-	54% inhibition at 5 mM leucine in the growth medium	658372	2D-image
N2	Azotobacter vinelandii	-	inhibits the C2H2 reduction	440183, 440189	2D-image
N2	Azotobacter vinelandii	-	inhibits C2H2 reduction of mutant H195Q; maximal inhibition of H2 production at Fe protein to MoFe protein ration 2.5	440184	2D-image
N2	Azotobacter vinelandii	-	competitive inhibition of acetylene reduction	658040	2D-image
N2	Azotobacter vinelandii	-	inhibits hydrazine reduction	659426	2D-image
N3-	Azotobacter vinelandii	-	inhibits H2 production competitively and reversibly	440184	2D-image
NaCl	Gluconacetobacter diazotrophicus	-	half-maximal inhibition at 100 mM	672344	2D-image
NAD+-malic enzyme	Mesorhizobium 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, overview	716483	-
NH4+	Rhodobacter capsulatus, Rhodospirillum rubrum	-	immediate inhibition, repression of induction	440142	2D-image
NH4+	Beggiatoa alba	-	immediate inhibition, repression of induction	440160	2D-image
NH4+	Gluconacetobacter diazotrophicus	-	18% inhibition at 5 mM, 32% at 15 mM ammonium in the growth medium	658372	2D-image
NH4Cl	Azoarcus sp.	-	nitrogenase activity is repressed by the addition of 0.5 mM NH4Cl	698619	2D-image
NIFI1,2	Methanococcus 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 vivo	684881	-
nitrate	Lotus 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 nitrate	699812	2D-image
NO	Azotobacter vinelandii	-	-	440154	2D-image
NO3-	Gluconacetobacter diazotrophicus	-	17% inhibition at 15 mM nitrate in the growth medium	658372	2D-image
O2	Klebsiella pneumoniae	-	complete reversible inhibition, reversibility decreases by increasing the time of exposure to O2	440140	2D-image
O2	Klebsiella pneumoniae	-	-	440142, 440147, 440149	2D-image
O2	Azotobacter vinelandii	-	-	440142, 440147, 440154	2D-image
O2	Clostridium pasteurianum	-	-	440142, 440147	2D-image
O2	Paenibacillus polymyxa	-	-	440147	2D-image
O2	Cyanobacterium sp.	-	irreversibly inactivated	440148	2D-image
phosphate	Azotobacter vinelandii	-	above 30 mM	440158	2D-image
SCN-	Azotobacter vinelandii	-	above 6 mM occurs substrate inhibition	440178	2D-image
sodium nitroprusside	Lotus japonicus	-	influence of the NO donor sodium nitroprusside on the relative levels of acetylene reduction activity, overview	699812	2D-image
tetrafluoroaluminate	Azotobacter vinelandii	P00459	inhibits by trapping of a stable Fe protein-MoFe protein nitrogenase complex, binds to the Fe protein	658483	2D-image
tungstate	Rhodobacter capsulatus	-	30% inhibition at 0.01 mM, 50% inhibition at 0.1 mM, 95% inhibition at 1 mM, inhibits MoFe protein expression	657985	2D-image
Urea	Beggiatoa alba	-	immediate inhibition, repression of induction	440160	2D-image
Vanadium	Azotobacter 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 Mo	440150	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, overview	687822	2D-image
Zn2+	Azotobacter vinelandii	-	-	440154	2D-image
MgADP	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	-	-	440146	2D-image
additional information	Azotobacter vinelandii	-	high ionic strength inhibits	440154	-
additional information	Azotobacter vinelandii	-	e.g. above 50 mM NaCl; high ionic strength inhibits	440158	-
additional information	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	overview	440174	-
additional information	Gluconacetobacter diazotrophicus	-	enzyme activity and bacterial growth is affected by amino acids in the growth medium	658372	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
C2H2	Azotobacter vinelandii	-	enhances the CH4 production but not NH3 production from CN-, wild-type enzyme	440181	2D-image
homocitrate	Azotobacter 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-fluorohomocitrate	440186	2D-image
light	Azotobacter 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, overview	715263	-
molybdate	Rhodobacter capsulatus	-	induces MoFe protein expression	657985	2D-image
additional information	Rhodobacter capsulatus	-	Fe protein contains an adenine-like molecule, a pentose moiety and a phosphate residue covalently attached to the molecule	440142, 440171	-
additional information	Rhodospirillum rubrum	-	Fe protein contains an adenine-like molecule, a pentose moiety and a phosphate residue covalently attached to the molecule	440142	-
additional information	Azotobacter vinelandii	-	H2 generation activates N2 binding	658040	-
additional information	Bradyrhizobium japonicum	-	several organic acids highly stimulate the enzyme activity of anaerobically isolated bacteroids, only malate has little effect	660287	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.3	-	ATP	Azotobacter vinelandii	-	-	440154	2D-image
0.3	-	ATP	Azotobacter vinelandii	-	with C2H2	440158	2D-image
0.3	-	C2H2	Azotobacter vinelandii	-	-	440158	2D-image
0.4	1.2	C2H2	Azotobacter vinelandii	-	-	440154	2D-image
0.45	-	CH4	Azotobacter vinelandii	-	mutant H195Q	440181	2D-image
1.6	-	CH4	Azotobacter vinelandii	-	wild-type	440181	2D-image
4.5	-	CH4	Azotobacter vinelandii	-	mutant H195N	440181	2D-image
0.1	-	N2	Azotobacter vinelandii	-	-	440154	2D-image
0.1	-	N2	Azotobacter vinelandii	-	with C2H2	440158	2D-image
0.9	-	SCN-	Azotobacter vinelandii	-	-	440178	2D-image
12	-	CH4	Azotobacter vinelandii	-	mutant Q191K	440181	2D-image
additional information	-	additional information	Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	-	440144	-
additional information	-	additional information	Azotobacter vinelandii	-	-	440154	-
additional information	-	additional information	Anabaena cylindrica	-	-	440170	-
additional information	-	additional information	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	overview, different substrates	440174	-
additional information	-	additional information	Rhodobacter capsulatus	-	-	440176	-
additional information	-	additional information	Azotobacter vinelandii	-	-	440183, 440184, 440189	-
additional information	-	additional information	Rhodobacter capsulatus	-	EPR signals of Mo and of W containing cofactor, redox potentials	657985	-
additional information	-	additional information	Azotobacter vinelandii	-	determination of EPR signals of wild-type enzyme and V70A mutant MoFe protein-containing enzyme with propargyl alcohol and C2H2 as substrates, temperature dependence	658010	-
additional information	-	additional information	Azotobacter vinelandii	P00459	redox properties of metal clusters and P-cluster, overview	658483	-
additional information	-	additional information	Klebsiella 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 measurements	658901	-
additional information	-	additional information	Azotobacter vinelandii	-	Km for N2 of wild-type and mutant enzyme	659426	-
additional information	-	additional information	Azotobacter vinelandii	-	kinetic analysis, overview	689764	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.3	-	SCN-	Azotobacter vinelandii	-	-	440178	2D-image
400	-	flavodoxin hydroquinone	Azotobacter vinelandii	-	before and after reduction of the nitrogenase complex relatively slow reactions take place, which limits the rate of the Fe protein cycle	440138	-
additional information	-	additional information	Azotobacter vinelandii	-	1200 per min: proton production of the reduced enzyme, MgATP-dependent	440175	-

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

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

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	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 atmosphere	440184
0.027	-	Klebsiella pneumoniae	-	reductant dithionite, whole cell assay	440140
0.066	-	Azotobacter vinelandii	-	crude extract, 100% Ar atmosphere, H2 production	440189
0.13	-	Azotobacter vinelandii	-	V70I mutant, substrate acetylene, in presence of C2H4	659426
0.17	-	Azotobacter vinelandii	-	V70I mutant, substrate N2, in presence of NH3	659426
0.2	-	Azotobacter vinelandii	-	wild-type enzyme, substrate acetylene, in presence of H2	659426
0.235	-	Rhodobacter capsulatus	-	substrate N2, purified Mo nitrogenase	440176
0.26	-	Rhodobacter capsulatus	-	substrate C2H2, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1	440176
0.27	-	Azotobacter vinelandii	-	mutant A175G, purified enzyme, substrate C2H2	440182
0.35	-	Rhodobacter capsulatus	-	substrate N2, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1	440176
0.43	-	Rhizobium lupini	-	purified Fe protein	440165
0.6	0.8	Rhodobacter capsulatus	-	purified Fe protein	440171
0.6	-	Azotobacter vinelandii	-	wild-type enzyme, substrate N2, in presence of NH3	659426
0.64	-	Azotobacter vinelandii	-	wild-type enzyme, substrate N2, in presence of H2	659426
0.7	-	Rhizobium lupini	-	purified MoFe protein	440165
0.7	-	Azotobacter vinelandii	-	purified enzyme, anaerobic atmosphere	440184
1.01	-	Azotobacter vinelandii	-	purified MoFe protein	440163
1.07	-	Xanthobacter autotrophicus	-	purified MoFe protein	440168
1.2	-	Clostridium pasteurianum	-	purified MoFe protein	440159
1.2	-	Rhodobacter capsulatus	-	substrate C2H2, purified Mo nitrogenase	440176
1.26	-	Xanthobacter autotrophicus	-	purified Fe protein	440168
1.3	-	Rhodobacter capsulatus	-	substrate H+, purified Mo nitrogenase	440176
1.5	1.7	Rhodobacter capsulatus	-	purified MoFe protein	440171
1.52	-	Azotobacter vinelandii	-	wild-type, purified enzyme, substrate C2H2	440182
1.6	-	Gluconacetobacter diazotrophicus	-	30�C, pH 7.5	672344
1.7	2.2	Clostridium pasteurianum	-	purified Fe protein	440159
1.8	-	Azospirillum amazonense	-	purified Fe protein	440161
1.8	-	Azotobacter vinelandii	-	wild-type enzyme, substrate acetylene, in presence of C2H4	659426
1.94	-	Azotobacter vinelandii	-	V70I mutant, substrate N2, in presence of H2	659426
2	-	Azotobacter vinelandii	-	wild-type enzyme, C2H2 reduction	658010
2	-	Azotobacter vinelandii	-	V70I mutant, substrate acetylene, in presence of H2	659426
2.01	-	Azotobacter vinelandii	-	purified Fe protein	440163
2.02	-	Azotobacter vinelandii	-	wild-type enzyme, substrate argon, in presence of H2	659426
2.082	-	Klebsiella pneumoniae	-	purified component II	440157
2.16	-	Klebsiella pneumoniae	-	purified component I	440157
2.2	-	Azotobacter vinelandii	P07328	about, micromol/min/mg MoFe protein, mutant enzyme, pH not specified in the publication, temperature not specified in the publication	715813
2.27	2.28	Azotobacter vinelandii	-	purified enzyme, substrate acetylene	440178
2.316	-	Azotobacter vinelandii	P07328	about, micromol/min/mg MoFe protein, wild-type enzyme, pH not specified in the publication, temperature not specified in the publication	715813
2.34	-	Azotobacter vinelandii	-	V70I mutant, substrate argon, in presence of H2	659426
2.4	-	Azospirillum amazonense	-	purified MoFe protein	440161
2.4	-	Rhodobacter capsulatus	-	substrate H+, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1	440176
additional information	-	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii	-	activity of Fe proteins and MoFe proteins	440143
additional information	-	Bradyrhizobium japonicum	-	-	440143
additional information	-	Clostridium pasteurianum, Klebsiella pneumoniae	-	activity of Fe proteins and MoFe proteins	440143
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; overview	440174
additional information	-	Rhodobacter capsulatus	-	-	440176
additional information	-	Azotobacter vinelandii	-	assay in anaerobic atmosphere required	440182, 440184
additional information	-	Azotobacter vinelandii	-	assay in anaerobic atmosphere required; wild-type and diverse alpha-His195 MoFe protein mutants	440189
additional information	-	Gluconacetobacter diazotrophicus	-	in vivo activity measurement, quantification of ethylene	658372
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, overview	713837
additional information	-	Klebsiella pneumoniae	-	comparison of ATP consumption coupled to H2 production by recombinant NifDK/NifB-co and by NifDK, overview	715017
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 nitrogenases	716922

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	8	Beggiatoa alba	-	-	440160
6.5	-	Azotobacter vinelandii	-	SCN- reduction	440178
7	8	Azotobacter vinelandii	-	assay at, hydrazine reduction activity	659426
7	-	Azotobacter vinelandii	-	assay at	658010
7	-	Azotobacter vinelandii	-	assay at, N2 reduction activity	659426
7.1	7.3	Xanthobacter autotrophicus	-	with substrates: N2, C2H2	440168
7.3	-	Azotobacter vinelandii	-	-	440158
7.4	-	Klebsiella pneumoniae	-	assay at	440157
7.4	-	Azotobacter vinelandii	-	assay at	440163, 440181, 440182
7.5	-	Methanococcus maripaludis	-	assay at, acetylene reduction	684881
8	-	Klebsiella pneumoniae	-	assay at	658901

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	8.3	Xanthobacter autotrophicus	-	pH 6.5: no activity below, pH 8.3: about 70% of activity maximum	440168
6.5	8.5	Rhodobacter capsulatus	-	below and above no remaining activity	440176
7.3	-	Gluconacetobacter diazotrophicus	-	narrow range	672344

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
15	40	Azotobacter vinelandii	-	no maximum with Ti3+ as reductant	440180
25	-	Azotobacter vinelandii	-	assay at	658010
25	-	Klebsiella pneumoniae	-	assay at	658901
29	-	Beggiatoa alba	-	-	440160
30	-	Klebsiella pneumoniae	-	assay at	440157
30	-	Azotobacter vinelandii	-	assay at	440158
30	-	Azospirillum amazonense	-	assay at	440161
30	-	Rhizobium sp.	-	assay at	440162
30	-	Azotobacter vinelandii	-	assay at	440163, 440180
30	-	Clostridium pasteurianum	-	assay at	440180
30	-	Azotobacter vinelandii	-	assay at	440181, 440182
30	-	Gluconacetobacter diazotrophicus	-	in vivo assay at	658372
30	-	Azotobacter vinelandii	-	assay at	659426
additional information	-	Azotobacter vinelandii	-	-	440184

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
13	45	Azotobacter vinelandii	-	-	440184
15	40	Azotobacter vinelandii	-	no maximum with Ti3+ as reductant	440180

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
root nodule	Rhizobium lupini	-	bacteroid	440143, 440165
root nodule	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae	-	bacteroid	440143
root nodule	Lotus japonicus	-	-	699812
heterocyst	Cyanobacterium sp.	-	in heterocysteous cyanobacteria exclusive site of N2 fixation during aerobic growth	440148
additional information	Anabaena sp.	-	the enzyme is localized to the microaerobic environment of heterocysts, a highly differentiated subset of the filamentous cells	713837
additional information	Crocosphaera watsonii	-	highest nitrogenase activity is observed at 29�C growth temperature. At 31�C 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	714845
additional information	Gloeothece sp.	-	highest nitrogenase activity is observed at 29�C growth temperature. At 31�C and above, nitrogenase activity is not detected 41�C and above. Enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview	714845
additional information	Mesorhizobium loti	-	cultivated as symbiont in Lotus japonicus root nodules	716483

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
cytosol	Lotus japonicus	-	-	5829	699812
additional information	Allochromatium 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	-	440144

PDB	SCOP	CATH	ORGANISM
1de0, download	SCOP (1de0)	CATH (1de0)	Azotobacter vinelandii
1fp4, download	SCOP (1fp4)	CATH (1fp4)	Azotobacter vinelandii
1fp6, download	SCOP (1fp6)	CATH (1fp6)	Azotobacter vinelandii
1g1m, download	SCOP (1g1m)	CATH (1g1m)	Azotobacter vinelandii
1g20, download	SCOP (1g20)	CATH (1g20)	Azotobacter vinelandii
1g21, download	SCOP (1g21)	CATH (1g21)	Azotobacter vinelandii
1g5p, download	SCOP (1g5p)	CATH (1g5p)	Azotobacter vinelandii
1l5h, download	SCOP (1l5h)	CATH (1l5h)	Azotobacter vinelandii
1m1n, download	SCOP (1m1n)	CATH (1m1n)	Azotobacter vinelandii
1m1y, download	SCOP (1m1y)	CATH (1m1y)	Azotobacter vinelandii
1m34, download	SCOP (1m34)	CATH (1m34)	Azotobacter vinelandii
1n2c, download	SCOP (1n2c)	CATH (1n2c)	Azotobacter vinelandii
1rw4, download	SCOP (1rw4)	CATH (1rw4)	Azotobacter vinelandii
1xcp, download	SCOP (1xcp)	CATH (1xcp)	Azotobacter vinelandii
1xd8, download	SCOP (1xd8)	CATH (1xd8)	Azotobacter vinelandii
1xd9, download	SCOP (1xd9)	CATH (1xd9)	Azotobacter vinelandii
1xdb, download	SCOP (1xdb)	CATH (1xdb)	Azotobacter vinelandii
2afh, download	SCOP (2afh)	CATH (2afh)	Azotobacter vinelandii
2afi, download	SCOP (2afi)	CATH (2afi)	Azotobacter vinelandii
2afk, download	SCOP (2afk)	CATH (2afk)	Azotobacter vinelandii
2c8v, download	SCOP (2c8v)	CATH (2c8v)	Azotobacter vinelandii
2min, download	SCOP (2min)	CATH (2min)	Azotobacter vinelandii
2nip, download	SCOP (2nip)	CATH (2nip)	Azotobacter vinelandii
3k1a, download	SCOP (3k1a)	CATH (3k1a)	Azotobacter vinelandii
3min, download	SCOP (3min)	CATH (3min)	Azotobacter vinelandii
3u7q, download	SCOP (3u7q)	CATH (3u7q)	Azotobacter vinelandii
1cp2, download	SCOP (1cp2)	CATH (1cp2)	Clostridium pasteurianum
1h1l, download	SCOP (1h1l)	CATH (1h1l)	Klebsiella pneumoniae
1qgu, download	SCOP (1qgu)	CATH (1qgu)	Klebsiella pneumoniae
1qh1, download	SCOP (1qh1)	CATH (1qh1)	Klebsiella pneumoniae
1qh8, download	SCOP (1qh8)	CATH (1qh8)	Klebsiella pneumoniae
1lfx, download	SCOP (1lfx)	CATH (1lfx)	Rhizobium sp. cowpea (strain IRc78)

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
35000	40000	Azotobacter vinelandii	-	Fe protein	440174
40000	74000	Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini	-	Fe protein: various methods, overview	440143
40000	74000	Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini	-	Fe protein: various methods, overview	440144
40000	-	Clostridium pasteurianum	-	Fe protein, ultracentrifugation	440144
44000	-	Azotobacter vinelandii	-	FeMo cofactor-NafY protein complex, gel filtration	659338
46000	-	Azotobacter vinelandii	-	NafY protein, gel filtration, sedimentation equilibrium centrifugation	659338
51000	-	Bradyrhizobium japonicum	-	Fe protein, gel filtration	440144
55000	60000	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	component II Fe protein	440147
55000	60000	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	component II Fe protein	440174
56000	-	Clostridium pasteurianum	-	Fe protein, gel filtration	440144, 440164
60000	-	Cyanobacterium sp.	-	Fe protein	440148
60000	-	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum	-	about; Fe protein	440186
61500	-	Rhodospirillum rubrum	-	Fe protein	440142
62000	-	Klebsiella pneumoniae	-	Fe protein, gel filtration	440144, 440149
63000	-	Azotobacter vinelandii	-	Fe protein	440138, 440142
63000	-	Rhodobacter capsulatus	-	Fe protein	440142, 440171
63000	-	Azotobacter vinelandii	-	Fe protein	440187
64000	-	Azotobacter chroococcum, Azotobacter vinelandii	-	Fe protein, gel filtration	440144
64000	-	Azotobacter chroococcum	-	Fe protein, gel filtration	440167
65000	-	Rhizobium lupini	-	Fe protein, gel filtration	440144, 440165
66800	-	Klebsiella pneumoniae	-	Fe protein	440174
68200	-	Klebsiella pneumoniae	-	Fe protein, ultracentrifugation	440144
74000	-	Rhizobium sp.	-	Fe protein, gel filtration	440162
160000	270000	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini	-	MoFe protein: various methods, overview	440143
160000	270000	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium lupini	-	MoFe protein: various methods, overview	440144
160000	-	Allochromatium vinosum	-	MoFe protein, estimation from Mo content, ultracentrifugation	440144
168000	-	Clostridium pasteurianum	-	MoFe protein, ultracentrifugation	440143
180000	-	Bradyrhizobium japonicum	-	MoFe protein, gel filtration	440143
194000	-	Rhizobium lupini	-	MoFe protein, gel filtration	440143, 440165
200000	250000	Rhodobacter capsulatus	-	tungsten-substituted enzyme component, gel filtration	657985
200000	-	Bradyrhizobium japonicum	-	-	440143
200000	-	Clostridium pasteurianum	-	MoFe protein, gel filtration	440143
200000	-	Klebsiella pneumoniae	-	-	440143
200000	-	Bradyrhizobium japonicum	-	MoFe protein, ultracentrifugation	440144
200000	-	Clostridium pasteurianum	-	-	440144
200000	-	Klebsiella pneumoniae	-	MoFe protein, ultracentrifugation	440144
210000	-	Clostridium pasteurianum	-	MoFe protein, gel filtration	440164
216000	-	Azotobacter vinelandii	-	MoFe protein, gel filtration	440143
216000	-	Cyanobacterium sp.	-	nitrogenase complex	440148
219000	-	Rhizobium sp.	-	MoFe protein, gel filtration	440162
220000	250000	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	component I MoFe protein	440147
220000	-	Klebsiella pneumoniae	-	MoFe protein, gel filtration	440149
220000	-	Anabaena cylindrica	-	MoFe protein, gel filtration	440170
226000	-	Klebsiella pneumoniae	-	MoFe protein, gel filtration	440143
227000	-	Azotobacter chroococcum	-	MoFe protein, gel filtration	440167
230000	-	Azotobacter vinelandii	-	MoFe protein	440138, 440142
230000	-	Rhodobacter capsulatus, Rhodospirillum rubrum	-	MoFe protein	440142
230000	-	Rhodobacter capsulatus	-	MoFe protein	440171
230000	-	Azotobacter vinelandii	-	MoFe protein	440187
270000	-	Azotobacter vinelandii	-	MoFe protein, ultracentrifugation	440143, 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 complex	440142
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 complex	440142
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 complex	440149
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 composition	440174

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Azotobacter chroococcum	-	MoFe protein 4 * 60000 + Fe protein 2 * 30800, SDS-PAGE	440167
?	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-PAGE	440176
?	Gluconacetobacter diazotrophicus	-	component Gd1, subunits of 53000 and 57500 Da, component Gd2, subunits of 33000 Da, SDS-PAGE	672344
dimer	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae	-	-	440142, 440144, 440146
dimer	Allochromatium vinosum, Rhodospirillum rubrum	-	-	440142, 440144
dimer	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum	-	Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview	440143, 440145
dimer	Azotobacter chroococcum, Paenibacillus polymyxa	-	-	440144, 440146
dimer	Anabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens, Rhizobium lupini	-	-	440144
dimer	Anabaena cylindrica, Corynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus, Rhizobium sp.	-	Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview	440145
dimer	Rhizobium sp.	-	2 * 36000, SDS-PAGE	440162
dimer	Clostridium pasteurianum	-	2 * 27500, SDS-PAGE	440164
tetramer	Clostridium pasteurianum	-	-	440142, 440144, 440145, 440146
tetramer	Allochromatium vinosum, Azotobacter vinelandii, Klebsiella pneumoniae	-	MoFe protein is an alpha2beta2-tetramer	440142
tetramer	Rhodobacter capsulatus	-	alpha: 55000, beta: 59500; MoFe protein is an alpha2beta2-tetramer	440142
tetramer	Rhodospirillum rubrum	-	alpha: 58500, beta: 58500; MoFe protein is an alpha2beta2-tetramer	440142
tetramer	Azotobacter chroococcum, Azotobacter vinelandii, Klebsiella pneumoniae, Paenibacillus polymyxa	-	-	440144, 440145, 440146
tetramer	Allochromatium vinosum, Anabaena cylindrica, Bradyrhizobium japonicum, Corynebacterium flavescens, Rhizobium lupini, Rhodospirillum rubrum	-	-	440144, 440145
tetramer	Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Leptolyngbya boryana, Ornithopus sativus, Rhizobium sp.	-	-	440145
tetramer	Cyanobacterium sp.	-	-	440148
tetramer	Rhizobium sp.	-	alpha: 56000, beta: 59000	440162
tetramer	Clostridium pasteurianum	-	component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE	440164
tetramer	Rhodobacter capsulatus	-	MoFe protein 1 * 55000 + 1 * 59000 + Fe protein 2 * 33500, SDS-PAGE	440171
tetramer	Rhodobacter capsulatus	-	-	440176
tetramer	Rhodobacter capsulatus	-	tungsten-substituted enzyme component	657985
dimer	Azotobacter vinelandii	-	2 * 26141-28000, unassociated NafY protein, sequence calculation and sedimentation equilibrium centrifugation	659338
additional information	Azotobacter 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 substrates	440138
additional information	Clostridium pasteurianum	-	-	440142, 440145, 440159
additional information	Allochromatium 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 complex	440142
additional information	Paenibacillus polymyxa	-	-	440145, 440169
additional information	Anabaena cylindrica	-	-	440145, 440170
additional information	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Klebsiella pneumoniae, Rhizobium lupini, Rhodospirillum rubrum	-	-	440145
additional information	Azotobacter vinelandii	-	alpha-beta-monomer of the FeMo protein consists of the FeMo cofactor FeMo-co with the substrate reduction site and the [4Fe-4S] cluster	440146
additional information	Azospirillum amazonense	-	-	440161
additional information	Xanthobacter autotrophicus	-	-	440168
additional information	Rhodobacter capsulatus	-	-	440171
additional information	Azotobacter vinelandii	-	apo-MoFe protein has a alpha2beta2 subunit composition and interacts with Fe protein, can be rebuilt by addition of FeMo-cofactor	440179
additional information	Azotobacter vinelandii	-	VFe protein form 1 has alphabeta2 conformation, VFe protein form 2 has alpha2beta2 conformation	440188
additional information	Azotobacter vinelandii	P00459	overall 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 genes	658483
additional information	Azotobacter vinelandii	-	the NafY protein monomerizes upon binding to the FeMo cofactor	659338
additional information	Gluconacetobacter 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 4:1	672344
additional information	Klebsiella pneumoniae	-	Kp2 structure analysis bound to Vo2+, ATP, and ADP, characterization of the metal-nucleotide coordination environment, overview	687822
additional information	Klebsiella pneumoniae	-	Kp2 structure analysis bound to Vo2+ and at different pH, overview	687823
additional information	Azotobacter vinelandii	-	components of the electron transfer chains in nitrogenase and its homologue, overview	714796

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	Methanococcus 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 limitation	676049
additional information	Rhodospirillum rubrum	-	posttranslational regulation of nitrogenase is mediated via GlnD, a bifunctional uridylyltransferase/uridylyl-removing enzyme which is important in nitrogen assimilation and metabolism	662028

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Azotobacter vinelandii	-	440144, 440147
crystal structure analysis of the iron protein, and of the MoFe protein	Azotobacter vinelandii	P00459	658483
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 protein	Azotobacter 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 formation	Azotobacter 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, overview	Azotobacter vinelandii	P07328	715813
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 analysis	Clostridium 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, 4�C, X-ray diffraction structure determination and analysis at 2.85 A resolution	Methanocaldococcus jannaschii	-	713656

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
5	8	Azotobacter chroococcum	-	MoFe protein stable	440167
8.7	-	Azotobacter chroococcum	-	50% loss of activity after overnight dialysis at pH 8.7	440167

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
22	-	Azotobacter vinelandii	-	Fe protein, half-life: 18 h	440158
additional information	-	Azotobacter vinelandii	-	Fe protein: cold labile	440158

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
nitrogenase complex is more stable than either the MoFe protein or the Fe protein alone	Azotobacter vinelandii	-	440158
Fe protein is salt sensitive	Clostridium 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 O2	Allochromatium vinosum	-	440142, 440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Allochromatium vinosum	-	440143
extreme sensitivity to O2	Anabaena cylindrica	-	440144
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Anabaena sp., Anabaena variabilis	-	440166
stable to O2, no loss in nitrogen fixation activity	Anabaena variabilis	-	440148
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Azospirillum brasilense	-	440166
extreme sensitivity to O2	Azotobacter chroococcum	-	440143, 440144
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Azotobacter chroococcum	-	440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Azotobacter chroococcum	-	440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Azotobacter sp.	-	440166
extreme O2 lability, susceptibility to O2 increases with purification, but is retarded in presence of MgCl2	Azotobacter vinelandii	-	440158
extreme sensitivity to O2	Azotobacter vinelandii	-	440142, 440143, 440144
MoFe protein is extremely sensitive to O2	Azotobacter vinelandii	-	440147
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Azotobacter vinelandii	-	440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Azotobacter vinelandii	-	440143
enzyme is extremely oxygen-labile	Bradyrhizobium japonicum	-	660287
extreme sensitivity to O2	Bradyrhizobium japonicum	-	440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Bradyrhizobium japonicum	-	440143
extreme sensitivity to O2	Clostridium pasteurianum	-	440142, 440143, 440144
Fe protein is very O2 sensitive	Clostridium pasteurianum	-	440159
extreme sensitivity to O2	Corynebacterium flavescens	-	440144
extreme sensitivity to O2	Cyanobacterium sp.	-	440148
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Frankia 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 remains	Klebsiella pneumoniae	-	440140
extreme O2 lability, t1/2: 10 min, MoFe protein 45 s, Fe protein	Klebsiella pneumoniae	-	440149
extreme sensitivity to O2	Klebsiella pneumoniae	-	440142, 440143, 440144
MoFe protein is extremely sensitive to O2	Klebsiella pneumoniae	-	440147
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Klebsiella pneumoniae	-	440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Klebsiella pneumoniae	-	440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Oscillatoria sp.	-	440166
extreme sensitivity to O2	Paenibacillus polymyxa	-	440143, 440144
extreme O2 lability, t1/2: 1 min, Fe protein	Rhizobium lupini	-	440165
extreme sensitivity to O2	Rhizobium lupini	-	440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Rhizobium lupini	-	440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo	Rhizobium sp.	-	440166
extreme sensitivity to O2	Rhodobacter capsulatus	-	440142
extreme sensitivity to O2	Rhodospirillum rubrum	-	440142, 440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min	Rhodospirillum rubrum	-	440143

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

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Allochromatium vinosum	-	440143
-	Anabaena cylindrica	-	440170
strain Y1	Azospirillum amazonense	-	440161
-	Azotobacter chroococcum	-	440143
large scale	Azotobacter chroococcum	-	440167
partially, extraction of FeVco in an active form by N-methylformamide, and gel filtration of the reconstituted protein, overview	Azotobacter chroococcum	-	715261
-	Azotobacter vinelandii	-	440143, 440154, 440158, 440174, 440178
2 forms of VFe protein	Azotobacter vinelandii	-	440188
FeMo-cofactorless MoFe protein from nifB deletion mutant	Azotobacter vinelandii	-	440179
large scale; strict anaerobic conditions	Azotobacter vinelandii	-	440163
mutant betaG69S	Azotobacter vinelandii	P00459	658483
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 homogeneity	Azotobacter vinelandii	-	658010
strict anaerobic conditions	Azotobacter vinelandii	-	440153
wild-type and mutant H195Q	Azotobacter vinelandii	-	440184, 440189
wild-type and mutants H195Q, H195N, Q191K	Azotobacter vinelandii	-	440181
-	Clostridium pasteurianum	-	440143
all components	Clostridium pasteurianum	-	440164
strict anaerobic conditions	Clostridium pasteurianum	-	440153, 440159
-	Klebsiella pneumoniae	-	440143
both components	Klebsiella pneumoniae	-	440157
native NifDK by gel filtration and affinity chromatography on a NifB resin, elution as NifDK/NifB-co complex	Klebsiella pneumoniae	-	715017
purification of the enzyme complex and isolation of the MoFe protein thereof	Klebsiella pneumoniae	-	658901
recombinant His-tagged NifH2 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration to over 95% purity	Methanocaldococcus jannaschii	-	713656
-	Paenibacillus polymyxa	-	440169
both components	Rhizobium lupini	-	440165
ORS571	Rhizobium sp.	-	440162
-	Rhodobacter capsulatus	-	440171
iron-only nitrogenase, both components	Rhodobacter capsulatus	-	440176
molybdenum containing enzyme form, both components	Rhodobacter capsulatus	-	440177
wild-type and tungsten-substituted enzymes	Rhodobacter capsulatus	-	657985
both components	Xanthobacter 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 Blue	Anabaena 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 pneumoniae	Anabaena 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 protein	Azotobacter chroococcum	-	715261
expression of His-tagged wild-type and V70A mutant MoFe protein in strain DJ1310, expression of the wild-type Fe protein	Azotobacter vinelandii	-	658010
genetic analysis	Azotobacter vinelandii	-	440155
overexpression of Azotobacter vinelandii NafY protein in Escherichia coli strain BL21(DE3)	Azotobacter vinelandii	-	659338
expression in Escherichia coli	Bradyrhizobium japonicum	-	440151
expression of nitrogenase in the absence of NH4+ and at initial O2 concentrations above 5% in the culture atmosphere	Gluconacetobacter diazotrophicus	-	672344
genetic mapping	Herbaspirillum seropedicae	-	658769
phylogenetic analysis, overview	Klebsiella 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

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
F388 A	Anabaena 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, overview	713837
F388H	Anabaena 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, overview	713837
F388T	Anabaena 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, overview	713837
F388Y	Anabaena 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, overview	713837
H197A	Anabaena 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, overview	713837
H197D	Anabaena 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, overview	713837
H197E	Anabaena 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, overview	713837
H197F	Anabaena 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, overview	713837
H197G	Anabaena 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, overview	713837
H197K	Anabaena 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, overview	713837
H197L	Anabaena 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, overviewup	713837
H197N	Anabaena 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, overview	713837
H197Q	Anabaena 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, overview	713837
H197R	Anabaena 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, overview	713837
H197S	Anabaena 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, overview	713837
H197T	Anabaena 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, overview	713837
Q193A	Anabaena 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, overview	713837
Q193G	Anabaena 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, overview	713837
Q193H	Anabaena 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, overview	713837
Q193K	Anabaena 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, overview	713837
Q193L	Anabaena 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, overview	713837
Q193N	Anabaena 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, overview	713837
Q193S	Anabaena 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, overview	713837
Q193V	Anabaena 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, overview	713837
R284C	Anabaena 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, overview	713837
R284E	Anabaena 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, overview	713837
R284F	Anabaena 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, overview	713837
R284H	Anabaena 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, overview	713837
R284K	Anabaena 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, overview	713837
R284L	Anabaena 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, overview	713837
R284Q	Anabaena 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, overview	713837
R284T	Anabaena 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, overview	713837
R284Y	Anabaena 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, overview	713837
S285A	Anabaena 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, overview	713837
S285C	Anabaena 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, overview	713837
S285D	Anabaena 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, overview	713837
S285G	Anabaena 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, overview	713837
S285M	Anabaena 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, overview	713837
S285N	Anabaena 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, overview	713837
S285Q	Anabaena 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, overview	713837
S285T	Anabaena 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, overview	713837
Y236A	Anabaena 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, overview	713837
Y236D	Anabaena 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, overview	713837
Y236F	Anabaena 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, overview	713837
Y236H	Anabaena 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, overview	713837
Y236M	Anabaena 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, overview	713837
Y236N	Anabaena 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, overview	713837
A175G	Azotobacter 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 structures	440182
A175S	Azotobacter vinelandii	-	unable to support substrate reduction because of an inability to undergo a required MgATP-induced conformational change	440182
D125E	Azotobacter vinelandii	P00459	site-directed mutagenesis, mutation alters the properties of the MgATP2- binding site with bound MgADP	658483
G69S	Azotobacter vinelandii	P00459	random 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 enzyme	658483
H195G	Azotobacter vinelandii	-	alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, slightly decreased Fe protein activity, altered phenotype	440189
H195L	Azotobacter vinelandii	-	alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, increased Fe protein activity, altered phenotype	440189
H195N	Azotobacter 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 less	440181
H195N	Azotobacter vinelandii	-	alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, altered phenotype	440189
H195Q	Azotobacter vinelandii	-	alphaHis195 of MoFe protein, shows 159% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition	440181
H195Q	Azotobacter vinelandii	-	below 2% N2 reducing activity remaining compared to wild-type due to less effective N2 binding	440184
H195Q	Azotobacter vinelandii	-	alpha-His of MoFe protein, site directed mutagenesis, decreased MoFe protein activity, altered phenotype	440189
H195T	Azotobacter vinelandii	-	alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype	440189
H195Y	Azotobacter vinelandii	-	alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype	440189
Q191A/V70A	Azotobacter vinelandii	-	site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene	688191
Q191K	Azotobacter vinelandii	-	alphaGln191 of MoFe protein, shows 6% activity compared to wild-type, substrate CN-, not affected by addition of C2H2	440181
S188C	Azotobacter vinelandii	P00459	site-directed mutagenesis, mutation of a residue within the P-cluster of the beta-subunit, alters the EPR signal of the MoFe protein	658483
S69G	Azotobacter vinelandii	-	alpha-subunit MoFe protein, resistant to inhibition by C2H2, thus acetylene binding/reduction site is not directly relevant to the mechanism of nitrogen reduction	440183
V70A	Azotobacter 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 analysis	658010
V70A	Azotobacter vinelandii	-	site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme	659426
V70A	Azotobacter vinelandii	-	site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne	688191
V70A/H195Q	Azotobacter 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 adduct	672039
V70G	Azotobacter 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-butyne	688191
V70I	Azotobacter vinelandii	-	site-directed mutagenesis, decreased the hydrazine reduction activity	659426
V70I	Azotobacter vinelandii	-	site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene	688191
V70I	Azotobacter vinelandii	-	the mutant is suitable for analysis of reaction intermediates, since it exhibits the highest concentration of trapped H+-intermediate when turned over under Ar	689764
V70I	Azotobacter vinelandii	P07328	substitution 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 activity	715813
H197Y	Anabaena 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, overview	713837
additional information	Anabaena sp.	-	engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview	713837
Y236T	Anabaena 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, overview	713837
additional information	Azospirillum 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 delayed	673723
K15Q	Azotobacter vinelandii	P00459	site-directed mutagenesis, mutation inhibits the communication of the [4Fe4S] cluster with the MgATP2- binding site	658483
additional information	Azotobacter vinelandii	-	construction of mutant strain RP114	440155
additional information	Azotobacter vinelandii	-	natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster	440179
additional information	Azotobacter vinelandii	-	-	440183
additional information	Azotobacter vinelandii	P00459	deletion 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 protein	658483
additional information	Azotobacter 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 insertion	676778
additional information	Azotobacter 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, overview	688191
additional information	Azotobacter 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, overview	689764
additional information	Azotobacter 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, overview	715263
V70X	Azotobacter 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 hydrazine	659426
additional information	Bradyrhizobium japonicum	-	transposon insertion mutants of several plasmids	440151
additional information	Herbaspirillum seropedicae	-	strains mutated in the nifX or orf1 genes show 90% or 50% reduction in nitrogenase activity under low levels of iron or molybdenum, respectively	658769
additional information	Klebsiella 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 NH3	715017
additional information	Rhodobacter 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 modABCD	440176

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
native enzyme is reconstituted from N-methylformamide extraction	Azotobacter 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 2134	Bradyrhizobium japonicum	-	660287

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
agriculture	Alnus 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 zone	676442
energy production	Azotobacter vinelandii	-	the reaction produces H2 as a by-product and is interesting for production of clean energy	689764

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
440134	Haaker, H.; Klugkist, J.	The bioenergetics of electron transport to nitrogenase	FEMS Microbiol. Rev.	46	57-71	1987	Anabaena 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	-
440138	Duyvis, M.G.; Wassink, H.; Haaker, H.	Nitrogenase of Azotobacter vinelandii: kinetic analysis of the Fe protein redox cycle	Biochemistry	37	17345-17354	1998	Azotobacter vinelandii	PubMed
440140	Kavanagh, E.P.; Hill, S.	Oxygen inhibition of nitrogenase activity in Klebsiella pneumoniae	J. Gen. Microbiol.	139	1307-1314	1992	Klebsiella pneumoniae	PubMed
440142	Vignais, P.M.; Colbeau, A.; Willison, J.C.; Jouanneau, Y.	Hydrogenase, nitrogenase, and hydrogen metabolism in the photosynthetic bacteria	Adv. Microb. Physiol.	26	155-234	1985	Allochromatium vinosum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Rhodobacter capsulatus, Rhodospirillum rubrum	PubMed
440143	Eady, R.R.	Isolation and characterization of various nitrogenases	Methods Enzymol.	69	753-778	1980	Allochromatium vinosum, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum	-
440144	Winter, H.C.; Burris, R.H.	Nitrogenase	Annu. Rev. Biochem.	45	409-426	1976	Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Klebsiella pneumoniae, Paenibacillus polymyxa, Rhizobium lupini, Rhodospirillum rubrum	PubMed
440145	Eady, R.R.; Postgate, J.R.	Nitrogenase	Nature	249	805-810	1974	Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Klebsiella pneumoniae, Leptolyngbya boryana, Ornithopus sativus, Paenibacillus polymyxa, Rhizobium lupini, Rhizobium sp., Rhodospirillum rubrum	PubMed
440146	Mortenson, L.E.; Thorneley, R.N.F.	Structure and function of nitrogenase	Annu. Rev. Biochem.	48	387-418	1979	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	PubMed
440147	Shah, V.K.; Ugalde, R.A.; Imperial, J.; Brill, W.J.	Molybdenum in nitrogenase	Annu. Rev. Biochem.	53	231-257	1984	Azotobacter vinelandii, Clostridium pasteurianum, Klebsiella pneumoniae, Paenibacillus polymyxa	PubMed
440148	Houchins, J.P.	The physiology and biochemistry of hydrogen metabolism in cyanobacteria	Biochim. Biophys. Acta	768	227-255	1984	Anabaena variabilis, Cyanobacterium sp.	-
440149	Palmer, G.	Iron-sulfur proteins	The Enzymes, 3rd Ed. (Boyer, P.D., ed.)	12	1-56	1975	Klebsiella pneumoniae	-
440150	Pau, R.N.	Nitrogenases without molybdenum	Trends Biochem. Sci.	14	183-186	1989	Azotobacter chroococcum, Azotobacter vinelandii	PubMed
440151	Fuhrmann, M.; Hennecke, H.	Coding properties of cloned nitrogenase structural genes from Rhizobium japonicum	Mol. Gen. Genet.	187	419-425	1982	Bradyrhizobium japonicum	-
440152	Hirschberg, R.; Samson, S.M.; Kimmel, B.E.; Page, K.A.; Collins, J.J.; Myers, J.A.; Yarbrough, L.R.	Cloning and characterization of nitrogenase genes from Anabaena variabilis	J. Biotechnol.	2	23-37	1985	Anabaena variabilis, Klebsiella pneumoniae	-
440153	Weininger, M.S.; Mortenson, L.E.	Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii	Proc. Natl. Acad. Sci. USA	79	379-380	1982	Azotobacter vinelandii, Clostridium pasteurianum	-
440154	Burns, R.C.; Hardy, R.W.F.	Purification of nitrogenase and crystallization of its Mo-Fe protein	Methods Enzymol.	24	480-496	1972	Azotobacter vinelandii	PubMed
440155	Pau, R.N.; Mitchenall, L.A.; Robson, R.L.	Genetic evidence for an Azotobacter vinelandii nitrogenase lacking molybdenum and vanadium	J. Bacteriol.	171	124-129	1989	Azotobacter vinelandii	PubMed
440156	Morningstar, J.E.; Johnson, M.K.; Case, E.E.; Hales, B.J.	Characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins of Azotobacter vinelandii using magnetic circular dichroism spectroscopy	Biochemistry	26	1795-1800	1987	Azotobacter vinelandii	PubMed
440157	Shah, V.K.	Isolation and characterization of nitrogenase from Klebsiella pneumoniae	Methods Enzymol.	118	511-519	1986	Klebsiella pneumoniae	PubMed
440158	Bulen, W.A.; LeComte, J.R.	Nitrogenase complex and its components	Methods Enzymol.	24B	456-470	1972	Azotobacter vinelandii	PubMed
440159	Mortenson, L.E.	Purification aof nitrogenase from Clostridium pasteurianum	Methods Enzymol.	24B	446-456	1972	Clostridium pasteurianum	PubMed
440160	Polman, J.K.; Larkin, J.M.	Properties of in vivo nitrogenase activity in Beggiatoa alba	Arch. Microbiol.	150	126-130	1988	Beggiatoa alba	-
440161	Song, S.D.; Hartmann, A.; Burris, R.H.	Purification and properties of the nitrogenase of Azospirillum amazonense	J. Bacteriol.	164	1271-1277	1985	Azospirillum amazonense	PubMed
440162	Kush, A.; Elmerich, C.; Aubert, J.P.	Nitrogenase of Sesbania Rhizobium strain ORS571: purification, properties, and 'switch-off' by ammonia	J. Gen. Microbiol.	131	1765-1777	1985	Rhizobium sp.	-
440163	Burgess, B.K.; Jacobs, D.B.; Stiefel, E.I.	Large-scale purification of high activity Azotobacter vinelandii nitrogenase	Biochim. Biophys. Acta	614	196-209	1980	Azotobacter vinelandii	PubMed
440164	Tso, M.Y.W.	Some properties of the nitrogenase proteins from Clostridium pasteurianum. Molecular weight, subunit structure, isoelectric point and EPR spectra	Arch. Microbiol.	99	71-80	1974	Clostridium pasteurianum	PubMed
440165	Whitting, M.J.; Dilworth, M.J.	Legume root nodule nitrogenase. Purification, properties, and studies on its genetic control	Biochim. Biophys. Acta	371	337-351	1974	Rhizobium lupini	PubMed
440166	Oelze, J.	Mechanismen zum Schutz der Sauerstoff-labilen Nitrogenase	Forum Mikrobiol.	4	116-126	1988	Anabaena sp., Anabaena variabilis, Azospirillum brasilense, Azotobacter chroococcum, Azotobacter sp., Azotobacter vinelandii, Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Oscillatoria sp., Rhizobium sp., Rhodospirillum rubrum	-
440167	Yates, M.G.; Planque, K.	Nitrogenase from Azotobacter chroococcum. Purification and properties of the component proteins	Eur. J. Biochem.	60	467-476	1975	Azotobacter chroococcum	PubMed
440168	Berndt, H.; Lowe, D.J.; Yates, M.G.	The nitrogen-fixing system of Corynebacterium autotrophicum. Purification and properties of the nitrogenase components and two ferredoxins	Eur. J. Biochem.	86	133-142	1978	Xanthobacter autotrophicus	PubMed
440169	Emerich, D.W.; Burris, R.H.	Nitrogenase from Bacillus polymyxa. Purification and properties of the component proteins	Biochim. Biophys. Acta	536	172-183	1978	Paenibacillus polymyxa	PubMed
440170	Hallenbeck, P.C.; Kostel, P.J.; Benemann, J.R.	Purification and properties of nitrogenase from the cyanobacterium, Anabaena cylindrica	Eur. J. Biochem.	98	275-284	1979	Anabaena cylindrica	PubMed
440171	Hallenbeck, P.C.; Meyer, C.; Vignais, P.M.	Nitrogenase from the photosynthetic bacterium Rhodopseudomonas capsulata: purification and molecular properties	J. Bacteriol.	149	708-717	1982	Rhodobacter capsulatus	PubMed
440174	Zumft, W.G.; Mortenson, L.E.	The nitrogen-fixing complex of bacteria	Biochim. Biophys. Acta	416	1-52	1975	Azotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.	PubMed
440175	Duyvis, M.G.; Wassink, H.; Haaker, H.	Pre-steady-state MgATP-dependent proton production and electron transfer by nitrogenase from Azotobacter vinelandii	Eur. J. Biochem.	225	881-890	1994	Azotobacter vinelandii	PubMed
440176	Schneider, K.; Gollan, U.; Drottboom, M.; Selsemeier-Voigt, S.; Muller, A.	Comparative biochemical characterization of the iron-only nitrogenase and the molybdenum nitrogenase from Rhodobacter capsulatus	Eur. J. Biochem.	244	789-800	1997	Rhodobacter capsulatus	PubMed
440177	Siemann, S.; Schneider, K.; Drottboom, M.; Muller, A.	The Fe-only nitrogenase and the Mo nitrogenase from Rhodobacter capsulatus: a comparative study on the redox properties of the metal clusters present in the dinitrogenase components	Eur. J. Biochem.	269	1650-1661	2002	Rhodobacter capsulatus	PubMed
440178	Rasche, M.E.; Seefeldt, L.C.	Reduction of thiocyanate, cyanate, and carbon disulfide by nitrogenase: kinetic characterization and EPR spectroscopic analysis	Biochemistry	36	8574-8585	1997	Azotobacter vinelandii	PubMed
440179	Christiansen, J.; Goodwin, P.J.; Lanzilotta, W.N.; Seefeldt, L.C.; Dean, D.R.	Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii	Biochemistry	37	12611-12623	1998	Azotobacter vinelandii	PubMed
440180	Erickson, J.A.; Nyborg, A.C.; Johnson, J.L.; Truscott, S.M.; Gunn, A.; Nordmeyer, F.R.; Watt, G.D.	Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants That form the all-ferrous redox state of the Fe protein	Biochemistry	38	14279-14285	1999	Azotobacter vinelandii, Clostridium pasteurianum	PubMed
440181	Fisher, K.; Dilworth, M.J.; Kim, C.H.; Newton, W.E.	Azotobacter vinelandii nitrogenases with substitutions in the FeMo-cofactor environment of the MoFe protein: effects of acetylene or ethylene on interactions with H+, HCN, and CN-	Biochemistry	39	10855-10865	2000	Azotobacter vinelandii	PubMed
440182	Bursey, E.H.; Burgess, B.K.	Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change	J. Biol. Chem.	273	16927-16934	1998	Azotobacter vinelandii	PubMed
440183	Christiansen, J.; Cash, V.L.; Seefeldt, L.C.; Dean, D.R.	Isolation and characterization of an acetylene-resistant nitrogenase	J. Biol. Chem.	275	11459-11464	2000	Azotobacter vinelandii	PubMed
440184	Dilworth, M.J.; Fisher, K.; Kim, C.H.; Newton, W.E.	Effects on substrate reduction of substitution of histidine-195 by glutamine in the alpha-subunit of the MoFe protein of Azotobacter vinelandii nitrogenase	Biochemistry	37	17495-17505	1998	Azotobacter vinelandii	PubMed
440186	Kim, J.; Rees, D.C.	Nitrogenase and biological nitrogen fixation	Biochemistry	33	389-397	1994	Azotobacter chroococcum, Azotobacter vinelandii, Clostridium pasteurianum	PubMed
440187	Johnson, J.L.; Tolley, A.M.; Erickson, J.A.; Watt, G.D.	Steady-state kinetic studies of dithionite utilization, component protein interaction, and the formation of an oxidized iron protein intermediate during Azotobacter vinelandii nitrogenase catalysis	Biochemistry	35	11336-11342	1996	Azotobacter vinelandii	PubMed
440188	Blanchard, C.Z.; Hales, B.J.	Isolation of two forms of the nitrogenase VFe protein from Azotobacter vinelandii	Biochemistry	35	472-478	1996	Azotobacter vinelandii	PubMed
440189	Kim, C.H.; Newton, W.E.; Dean, D.R.	Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis	Biochemistry	34	2798-2808	1995	Azotobacter vinelandii	PubMed
657985	Siemann, S.; Schneider, K.; Oley, M.; Muller, A.	Characterization of a tungsten-substituted nitrogenase isolated from Rhodobacter capsulatus	Biochemistry	42	3846-3857	2003	Rhodobacter capsulatus	PubMed
658010	Benton, P.M.; Laryukhin, M.; Mayer, S.M.; Hoffman, B.M.; Dean, D.R.; Seefeldt, L.C.	Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe protein	Biochemistry	42	9102-9109	2003	Azotobacter vinelandii	PubMed
658040	Seefeldt, L.C.; Dance, I.G.; Dean, D.R.	Substrate interactions with nitrogenase: Fe versus Mo	Biochemistry	43	1401-1409	2004	Azotobacter vinelandii	PubMed
658372	Tejera, N.A.; Ortega, E.; Rodes, R.; Lluch, C.	Influence of carbon and nitrogen sources on growth, nitrogenase activity, and carbon metabolism of Gluconacetobacter diazotrophicus	Can. J. Microbiol.	50	745-750	2004	Gluconacetobacter diazotrophicus	PubMed
658483	Igarashi, R.Y.; Seefeldt, L.C.	Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase	Crit. Rev. Biochem. Mol. Biol.	38	351-384	2003	Azotobacter vinelandii	PubMed
658769	Klassen, G.; de Oliveira Pedrosa, F.; de Souza, E.M.; Yates, M.G.; Rigo, L.U.	Nitrogenase activity of Herbaspirillum seropedicae grown under low iron levels requires the products of nifXorf1 genes	FEMS Microbiol. Lett.	224	255-259	2003	Herbaspirillum seropedicae	PubMed
658901	Cui, Z.; Dunford, A.J.; Durrant, M.C.; Henderson, R.A.; Smith, B.E.	Binding sites of nitrogenase: kinetic and theoretical studies of cyanide binding to extracted FeMo-cofactor derivatives	Inorg. Chem.	42	6252-6264	2003	Klebsiella pneumoniae	PubMed
659338	Rubio, L.M.; Singer, S.W.; Ludden, P.W.	Purification and characterization of NafY (apodinitrogenase gamma subunit) from Azotobacter vinelandii	J. Biol. Chem.	279	19739-19746	2004	Azotobacter vinelandii	PubMed
659426	Barney, B.M.; Igarashi, R.Y.; Dos Santos, P.C.; Dean, D.R.; Seefeldt, L.C.	Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis	J. Biol. Chem.	279	53621-53624	2004	Azotobacter vinelandii	PubMed
660287	Karr, D.B.; Oehrle, N.W.; Emerich, D.W.	Recovery of nitrogenase from aerobically isolated soybean nodule bacteroids	Plant Soil	257	27-33	2003	Bradyrhizobium japonicum	-
662028	Zhang, 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 rubrum	J. Bacteriol.	187	1254-1265	2005	Rhodospirillum rubrum	PubMed
672039	Barney, 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 site	Biochemistry	44	8030-8037	2005	Azotobacter vinelandii	PubMed
672344	Fisher, K.; Newton, W.E.	Nitrogenase proteins from Gluconacetobacter diazotrophicus, a sugarcane-colonizing bacterium	Biochim. Biophys. Acta	1750	154-165	2005	Gluconacetobacter diazotrophicus	PubMed
673039	Fisher, K.; Lowe, D.J.; Petersen, J.	Vanadium (V) is reduced by the 'as isolated' nitrogenase Fe-protein at neutral pH	Chem. Commun. (Camb.)	2006	2807-2809	2006	Azotobacter vinelandii	PubMed
673723	Huergo, 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 brasilense	FEMS Microbiol. Lett.	253	47-54	2005	Azospirillum brasilense	PubMed
674147	Dance, I.	The hydrogen chemistry of the FeMo-co active site of nitrogenase	J. Am. Chem. Soc.	127	10925-10942	2005	Azotobacter vinelandii	PubMed
674154	Lee, H.I.; Sorlie, M.; Christiansen, J.; Yang, T.C.; Shao, J.; Dean, D.R.; Hales, B.J.; Hoffman, B.M.	Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO	J. Am. Chem. Soc.	127	15880-15890	2005	Azotobacter vinelandii	PubMed
674202	Dance, I.	The mechanistically significant coordination chemistry of dinitrogen at FeMo-co, the catalytic site of nitrogenase	J. Am. Chem. Soc.	129	1076-1088	2007	Azotobacter vinelandii	PubMed
676049	Dodsworth, 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 maripaludis	Mol. Microbiol.	56	1527-1538	2005	Methanococcus maripaludis	PubMed
676442	Kratsch, H.A.; Graves, W.R.	Oxygen concentration affects nodule anatomy and nitrogenase activity of Alnus maritima	Plant Cell Environ.	28	688-696	2005	Alnus maritima	-
676778	Hu, Y.; Corbett, M.C.; Fay, A.W.; Webber, J.A.; Hedman, B.; Hodgson, K.O.; Ribbe, M.W.	Nitrogenase reactivity with P-cluster variants	Proc. Natl. Acad. Sci. USA	102	13825-13830	2005	Azotobacter vinelandii	PubMed
684881	Dodsworth, J.A.; Leigh, J.A.	NIFI1,2 inhibits nitrogenase by competing with Fe protein for binding to the MoFe protein	Biochem. Biophys. Res. Commun.	364	378-382	2007	Methanococcus maripaludis	PubMed
687822	Petersen, J.; Fisher, K.; Lowe, D.J.	Structural basis for VO2+ inhibition of nitrogenase activity (A): 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy	J. Biol. Inorg. Chem.	13	623-635	2008	Klebsiella pneumoniae	PubMed
687823	Petersen, J.; Mitchell, C.J.; Fisher, K.; Lowe, D.J.	Structural basis for VO(2+)-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe-protein identified by ENDOR spectroscopy	J. Biol. Inorg. Chem.	13	637-650	2008	Klebsiella pneumoniae	PubMed
688191	Dos Santos, P.C.; Mayer, S.M.; Barney, B.M.; Seefeldt, L.C.; Dean, D.R.	Alkyne substrate interaction within the nitrogenase MoFe protein	J. Inorg. Biochem.	101	1642-1648	2007	Azotobacter vinelandii	PubMed
689764	Curatti, L.; Hernandez, J.A.; Igarashi, R.Y.; Soboh, B.; Zhao, D.; Rubio, L.M.	In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins	Proc. Natl. Acad. Sci. USA	104	17626-17631	2007	Azotobacter vinelandii	PubMed
698619	Oetjen, J.; Reinhold-Hurek, B.	Characterization of the DraT/DraG system for posttranslational regulation of nitrogenase in the endophytic betaproteobacterium Azoarcus sp. strain BH72	J. Bacteriol.	191	3726-3735	2009	Azoarcus sp.	PubMed
699812	Kato, K.; Kanahama, K.; Kanayama, Y.	Involvement of nitric oxide in the inhibition of nitrogenase activity by nitrate in Lotus root nodules	J. Plant Physiol.	167	238-241	2010	Lotus japonicus	PubMed
713656	Huang, K.; Ma, J.; Yuan, Y.; Gao, Y.	Cloning, expression, purification, crystallization and preliminary crystallographic analysis of NifH2 from Methanocaldococcus jannaschii	Acta Crystallogr. Sect. F	67	133-135	2011	Methanocaldococcus jannaschii	PubMed
713837	Masukawa, H.; Inoue, K.; Sakurai, H.; Wolk, C.P.; Hausinger, R.P.	Site-directed mutagenesis of the Anabaena sp. strain PCC 7120 nitrogenase active site to increase photobiological hydrogen production	Appl. Environ. Microbiol.	76	6741-6750	2010	Anabaena sp.	PubMed
714796	Hu, Y.; Fay, A.W.; Lee, C.C.; Wiig, J.A.; Ribbe, M.W.	Dual functions of NifEN: insights into the evolution and mechanism of nitrogenase	Dalton Trans.	39	2964-2971	2010	Azotobacter vinelandii	PubMed
714845	Compaore, J.; Stal, L.	Oxygen and the light-dark cycle of nitrogenase activity in two unicellular cyanobacteria	Environ. Microbiol.	12	54-62	2010	Crocosphaera watsonii, Gloeothece sp.	PubMed
715017	Soboh, B.; Boyd, E.S.; Zhao, D.; Peters, J.W.; Rubio, L.M.	Substrate specificity and evolutionary implications of a NifDK enzyme carrying NifB-co at its active site	FEBS Lett.	584	1487-1492	2010	Klebsiella pneumoniae	PubMed
715261	Fay, A.W.; Blank, M.A.; Lee, C.C.; Hu, Y.; Hodgson, K.O.; Hedman, B.; Ribbe, M.W.	Characterization of isolated nitrogenase FeVco	J. Am. Chem. Soc.	132	12612-12618	2010	Azotobacter chroococcum	PubMed
715263	Roth, L.E.; Nguyen, J.C.; Tezcan, F.A.	ATP- and iron-protein-independent activation of nitrogenase catalysis by light	J. Am. Chem. Soc.	132	13672-13674	2010	Azotobacter vinelandii	PubMed
715813	Sarma, R.; Barney, B.; Keable, S.; Dean, D.; Seefeldt, L.; Peters, J.	Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha70Ile MoFe protein variant	J. Inorg. Biochem.	104	385-389	2010	Azotobacter vinelandii	PubMed
716483	Thapanapongworakul, N.; Nomura, M.; Shimoda, Y.; Sato, S.; Tabata, S.; Tajima, S.	NAD+-malic enzyme affects nitrogenase activity of Mesorhizobium loti bacteroids in Lotus japonicus nodules	Plant Biotechnol.	27	31-316	2010	Mesorhizobium loti	-
716922	Lee, C.C.; Hu, Y.; Ribbe, M.W.	Vanadium nitrogenase reduces CO	Science	329	642	2010	Azotobacter vinelandii	PubMed
716924	Kaiser, J.T.; Hu, Y.; Wiig, J.A.; Rees, D.C.; Ribbe, M.W.	Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase	Science	331	91-94	2011	Azotobacter vinelandii	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.18.6.1)

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)

All organisms
Allochromatium vinosum
Alnus maritima
Anabaena cylindrica
Anabaena sp.
Anabaena variabilis
Azoarcus sp.
Azoarcus sp. BH72
Azorhizobium caulinodans ORS571
Azospirillum amazonense
Azospirillum brasilense
Azospirillum sp.
Azotobacter chroococcum
Azotobacter chroococcum YM68A
Azotobacter sp.
Azotobacter vinelandii
Azotobacter vinelandii DJ1310
Beggiatoa alba
Bradyrhizobium japonicum
Chlorobium sp.
Chromatium sp.
Clostridium pasteurianum
Corynebacterium flavescens
Corynebacterium flavescens 301
Crocosphaera watsonii
Cyanobacterium sp.
Desulfovibrio desulfuricans
Desulfovibrio sp.
Endomycopsis fibuligera Y1
Escherichia coli
Escherichia coli C-M 74
Frankia sp.
Gloeocapsa sp.
Gloeothece sp.
Gloeothece sp. PCC6909
Gluconacetobacter diazotrophicus
Gluconacetobacter diazotrophicus PAL-5
Herbaspirillum seropedicae
Klebsiella pneumoniae
Klebsiella pneumoniae UN1217
Leptolyngbya boryana
Lotus japonicus
Mesorhizobium loti
Methanocaldococcus jannaschii
Methanococcus maripaludis
Ornithopus sativus
Oscillatoria sp.
Paenibacillus polymyxa
Rhizobium leguminosarum
Rhizobium lupini
Rhizobium sp.
Rhodobacter capsulatus
Rhodobacter capsulatus B10S
Rhodobacter sphaeroides
Rhodopseudomonas sp.
Rhodospirillum rubrum
Xanthobacter autotrophicus