Information on EC 1.18.6.1 - nitrogenase

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

EC NUMBER
COMMENTARY
1.18.6.1
-
RECOMMENDED NAME
GeneOntology No.
nitrogenase
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
show the reaction diagram
-
-
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme complex dissociation and association kinetics; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; Fe protein and MoFe protein are assumed to associate and dissociate to transfer a single electron to the substrates; mechanism, Fe protein cycle
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Cyanobacterium sp.
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism; structure of V-containing enzyme form
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
catalytic mechanism; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; MgATP/MgADP-dependent electron and proton transfer kinetics
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
iron-only enzyme is composed of 2 components: FeFe protein and Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; iron-only enzyme is composed of 2 components: FeFe protein and Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic electron flow from Fe protein to substrate via MoFe protein and MoFe protein-cofactor
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
C2H2 inhibition mechanism, structure model; enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
structure of V-containing enzyme form
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
theoretical mechanisms of substrate binding to molybdenum or iron in the FeMo cofactor, modeling
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
overall catalytic mechanism, overview, structures of active site metal clusters, interactions of substrate and active site, active site relevant residues are Arg96, Val70, Gly69, and His195, substrate binding mechanism of complex components, mechanism of MgATP hydrolysis and electron transfer, overview
P00459
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
the active site is located on the MoFe protein, active site structure and substrate binding mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
active site location
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
first introduction of H at the NFe7MoS9(homocitrate) active site is via a water chain terminating at water 679 to S3B of the my3-S atoms of the active site. Discussion of subsequent movement of the H atoms around the NFe7MoS9(homocitrate) preparatory to the binding and hydrogenation of N2 and other substrates. S2B has a modulatory function and is not an H-entry site
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
SEPR1 intermediate formed during turnover of the nitrogenase alpha-195Gln MoFe protein with C2H2 in H2O buffers, is a product complex with C2H4 bound as a ferracycle to a single Fe of the FeMo-cofactor active site. CO bridges two Fe of lo-Co, while the C2H4 of SEPR1 binds to one of these. Correlation with Lowe-Thorneley En kinetic state
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
theoretical investigation of the binding of N2 to the Fe7MoS9N(homocitrate)(cysteine)(histidine) active site, calculation of reaction profiles and activation energies for the association and dissociation of N2. An endo-ny1-N2 coordination at Fe6 is most probable
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
reaction mechanism, overview
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
reaction mechanism, determination of reaction intermediates, two-step relaxation of the nitrogenase H+/H+ intermediate during step-annealing,both steps show large solvent kinetic isotope effects, step A is the catalytically central state that is activated for N2 binding by the accumulation of 4 electrons, and step B accumulates 2 electrons, overview
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Azospirillum amazonense Y1
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195
Azotobacter vinelandii DJ1310
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Azotobacter vinelandii OP, Beggiatoa alba B18LD, Corynebacterium flavescens 301, Escherichia coli C-M 74
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
the active site is located on the MoFe protein, active site structure and substrate binding mechanism
Klebsiella pneumoniae M5a1
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Rhizobium sp. ORS571
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; iron-only enzyme is composed of 2 components: FeFe protein and Fe protein; iron-only enzyme is composed of 2 components: FeFe protein and Fe protein
Rhodobacter capsulatus B10S
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Chloroalkane and chloroalkene degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
nitrogen fixation
-
Nitrogen metabolism
-
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
dinitrogenase
-
-
EC 1.18.2.1
-
-
formerly
-
Mo-nitrogenase
-
-
Mo-nitrogenase
Azotobacter chroococcum YM68A
-
-
-
molybdenum nitrogenase
-
-
molybdenum nitrogenase
Klebsiella pneumoniae UN1217
-
-
-
molybdenum-containing nitrogenase
-
-
molybdenum-containing nitrogenase
Anabaena sp. PCC 7120
-
-
-
molybdenum-nitrogenase
-
-
NifDK
Klebsiella pneumoniae UN1217
-
-
-
nitrogenase Fe protein
-
-
nitrogenase Fe-protein
-
-
nitrogenase FeVco
-
-
nitrogenase FeVco
Azotobacter chroococcum YM68A
-
-
-
nitrogenase iron-protein
-
-
V-nitrogenase
-
-
V-nitrogenase
Azotobacter chroococcum YM68A
-
-
-
vanadium nitrogenase
-
-
vanadium-nitrogenase
-
-
vanadium-nitrogenase
Azotobacter chroococcum YM68A
-
-
-
molybdenum-nitrogenase
Azotobacter chroococcum YM68A
-
-
-
additional information
-
the nitrogenase complex is composed of 2 oxygen-labile metalloproteins: dinitrogenase and dinitrogenase reductase
additional information
-
the nitrogenase complex is composed of 2 oxygen-labile metalloproteins: dinitrogenase and dinitrogenase reductase
-
CAS REGISTRY NUMBER
COMMENTARY
9013-04-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC 7120
-
-
-
Manually annotated by BRENDA team
nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
strain BH72
-
-
Manually annotated by BRENDA team
strain BH72
-
-
Manually annotated by BRENDA team
Azospirillum amazonense Y1
strain Y1
-
-
Manually annotated by BRENDA team
contains Mo- and V-nitrogenases
-
-
Manually annotated by BRENDA team
nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
Azotobacter chroococcum YM68A
contains Mo- and V-nitrogenases
-
-
Manually annotated by BRENDA team
Azotobacter sp.
-
-
-
Manually annotated by BRENDA team
2 forms of VFe protein
-
-
Manually annotated by BRENDA team
2 forms of VFe protein; nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
; recombinant strain DJ1373 expressing mutant V70I
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
contains nif-encoded molybdenum nitrogenase and vnf-encoded V nitrogenase
-
-
Manually annotated by BRENDA team
molybdenum-dependent enzyme variant
-
-
Manually annotated by BRENDA team
nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
strain DJ1310
-
-
Manually annotated by BRENDA team
strain DJ995
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
Azotobacter vinelandii DJ1310
strain DJ1310
-
-
Manually annotated by BRENDA team
Azotobacter vinelandii DJ995
strain DJ995
-
-
Manually annotated by BRENDA team
Azotobacter vinelandii OP
strain OP
-
-
Manually annotated by BRENDA team
strain B18LD
-
-
Manually annotated by BRENDA team
strain B18LD
-
-
Manually annotated by BRENDA team
associated with Glycine max
-
-
Manually annotated by BRENDA team
nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
strains 110 or 2134, anaerobically and aerobically isolated bacteroid from nodules of soybean
-
-
Manually annotated by BRENDA team
Chromatium sp.
-
-
-
Manually annotated by BRENDA team
nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
Corynebacterium flavescens 301
301
-
-
Manually annotated by BRENDA team
a marine unicellular diazotrophic cyanobacterium
-
-
Manually annotated by BRENDA team
Crocosphaera watsonii WH8501
a marine unicellular diazotrophic cyanobacterium
-
-
Manually annotated by BRENDA team
Cyanobacterium sp.
-
-
-
Manually annotated by BRENDA team
Escherichia coli C-M 74
C-M 74
-
-
Manually annotated by BRENDA team
Gloeocapsa sp.
-
-
-
Manually annotated by BRENDA team
a terrestrial unicellular diazotrophic cyanobacterium
-
-
Manually annotated by BRENDA team
Gloeothece sp. PCC6909
a terrestrial unicellular diazotrophic cyanobacterium
-
-
Manually annotated by BRENDA team
expression of nitrogenase in the absence of NH4+ and at initial O2 concentrations above 5% in the culture atmosphere
-
-
Manually annotated by BRENDA team
strain PAL-5, in endosymbiosis with sugarcane, Saccharum officinarum
-
-
Manually annotated by BRENDA team
Gluconacetobacter diazotrophicus PAL-5
strain PAL-5, in endosymbiosis with sugarcane, Saccharum officinarum
-
-
Manually annotated by BRENDA team
nitrogen fixation complex is encoded on nif gene cluster
-
-
Manually annotated by BRENDA team
strain M5a1
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M5a1
strain M5a1
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae UN1217
-
-
-
Manually annotated by BRENDA team
inoculated with symbiont Mesorhizobium loti strain New Zealand Palmerston 2235
-
-
Manually annotated by BRENDA team
NifH2 is one of two homologues of NifH in Methanocaldococcus jannaschii
-
-
Manually annotated by BRENDA team
associated with Lupinus luteus
-
-
Manually annotated by BRENDA team
associated with Phaseolus aureus or Vigna sinensis
-
-
Manually annotated by BRENDA team
ORS571
-
-
Manually annotated by BRENDA team
ORS571, associated with Sesbania rostrata
-
-
Manually annotated by BRENDA team
Rhizobium sp. ORS571
ORS571
-
-
Manually annotated by BRENDA team
iron-only nitrogenase and molybdenum nitrogenase; nitrogen fixation complex is encoded on nif gene cluster; strain B10S
-
-
Manually annotated by BRENDA team
wild-type strain B10S, molybdenum-containing, nif-encoded enzyme variant
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus B10S
strain B10S
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
NifEN and MoFe protein have evolved from the replication and divergence of a common ancestral gene. NifEN is catalytically active early on in the course of evolution, when the mantle of earth is likely more reduced. Later, NifEN might have gradually evolved into an effective enzyme with a wide range of substrates, i.e. the MoFe protein, while in the meantime adjusting its own role toward synthesizing a catalytically more powerful cofactor, i.e. the iron-molybdenum cofactor
evolution
-
substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview
evolution
-
the ability of V nitrogenase to catalyze both CO and N2 reductions suggests a potential link between the evolution of carbon and nitrogen cycles
physiological function
-
nitrogenase, an oxygen-labile enzyme typically containing an iron-molybdenum cofactor active site, is responsible for nitrogen fixation producing photobiological H2 as a byproduct
physiological function
-
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
physiological function
-
the diminished H2 evolution by V nitrogenase originates from the diversion of electrons toward CO reduction, in contrast to the Mo nitrogenase
physiological function
Anabaena sp. PCC 7120
-
nitrogenase, an oxygen-labile enzyme typically containing an iron-molybdenum cofactor active site, is responsible for nitrogen fixation producing photobiological H2 as a byproduct
-
physiological function
Klebsiella pneumoniae UN1217
-
the conversion of N2 into NH3 is catalyzed by the nitrogenase enzyme, which is composed of two metalloproteins: NifDK, also termed dinitrogenase or MoFe protein, and NifH, also termed dinitrogenase reductase or Fe protein
-
evolution
Klebsiella pneumoniae UN1217
-
substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview
-
additional information
-
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
additional information
-
nitrogenase consists of the Fe protein, encoded by nifH, and the MoFe protein, encoded by nifD and nifK. The Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein, which is bound at the active site and alpha2beta2 heterotetramer with each nifD-encoded alpha subunit coordinating the FeMo cofactor that binds and reduces substrate, while alpha plus the nifK-encoded beta subunits coordinate the [8Fe-7S] P-cluster
additional information
-
primary sequences of NifEN and MoFe proteins
additional information
-
pattern of nitrogenase activity during the light-dark cycle, overview
additional information
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
additional information
-
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
additional information
-
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview
additional information
Anabaena sp. PCC 7120
-
nitrogenase consists of the Fe protein, encoded by nifH, and the MoFe protein, encoded by nifD and nifK. The Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein, which is bound at the active site and alpha2beta2 heterotetramer with each nifD-encoded alpha subunit coordinating the FeMo cofactor that binds and reduces substrate, while alpha plus the nifK-encoded beta subunits coordinate the [8Fe-7S] P-cluster
-
additional information
Crocosphaera watsonii WH8501, Gloeothece sp. PCC6909
-
pattern of nitrogenase activity during the light-dark cycle, overview
-
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)+ + ?
show the reaction diagram
-
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
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Chromatium sp.
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Cyanobacterium sp.
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
active site for acetylene reduction interacts not directly with N2 reduction
-
-
-
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
anaerobic atmosphere
reduction cycle continues until complete reduction of the substrate to ethane
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
ferredoxin is the main but not the essential electron donor for nitrogenase
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Corynebacterium flavescens 301
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
Escherichia coli C-M 74
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
show the reaction diagram
-
intermediate is a flavodoxin hydroquinone
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chromatium sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chromatium sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeocapsa sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
slow enzyme
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
1-propyne, 1-butyne and allene are reduced to the corresponding alkenes
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
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
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.
-
ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin, regulation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
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
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum amazonense Y1
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii OP
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp. ORS571
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp. ORS571
-
biological N2 fixation, ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens 301
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Escherichia coli C-M 74
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
P00459
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL-5
-
-
-
-
?
acetylene + ?
ethylene + ?
show the reaction diagram
Klebsiella pneumoniae M5a1
-
-
-
-
?
C2H2 + ?
?
show the reaction diagram
Azotobacter vinelandii, Azotobacter vinelandii DJ1310
-
-
-
-
?
C2H2 + ?
H2 + ?
show the reaction diagram
-
-
-
-
?
CS2 + ?
H2S + ?
show the reaction diagram
P00459
slow turnover
-
-
?
cyanamide + ?
?
show the reaction diagram
P00459
-
-
-
?
cyanide + ?
?
show the reaction diagram
P00459
-
-
-
?
cyanide + ?
?
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
-
cyanide favors the molydenum for binding
-
-
?
cyclopropene + ?
?
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
-
-
-
-
?
dithionite + H+ + acetylene + ATP
?
show the reaction diagram
Azospirillum amazonense, Azospirillum amazonense Y1
-
-
-
-
?
dithionite + H+ + N2 + ATP
?
show the reaction diagram
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
show the reaction diagram
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
show the reaction diagram
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
show the reaction diagram
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
show the reaction diagram
-
SO2- being the actual nitrogenase reductant, reaction kinetics
-
-
?
dithionite + H+ + N2 + ATP
?
show the reaction diagram
Azotobacter vinelandii OP
-
in vitro substrate
-
-
?
ethylene + ?
?
show the reaction diagram
-
-
-
-
?
ethylene + ?
?
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
-
-
-
-
?
hydrazine + ?
?
show the reaction diagram
-
high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme
-
-
?
methyl isocyanide + ?
?
show the reaction diagram
-
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
-
-, 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
-
-
?
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
-
-, cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview
-
-
ir
N2H4 + ?
?
show the reaction diagram
P00459
-
-
-
?
N2O + ?
?
show the reaction diagram
-
-
-
-
?
N2O + ?
?
show the reaction diagram
P00459
-
-
-
?
N3- + ?
?
show the reaction diagram
-
-
-
-
?
N3- + ?
?
show the reaction diagram
P00459
-
-
-
?
propargyl alcohol + ?
?
show the reaction diagram
Azotobacter vinelandii, Azotobacter vinelandii DJ1310
-
wild-type enzyme and V70A mutant MoFe protein-containing enzyme
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
-
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
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Corynebacterium flavescens 301
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Rhodobacter capsulatus B10S
-
H2-producing activity is much higher in the iron-only enzyme form than in the molybdenum containing form and is less inhibited by competitive substrates
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
show the reaction diagram
Escherichia coli C-M 74
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
Chromatium sp.
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
Chromatium sp.
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
P00459
enzyme complex is responsible for the majority of biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
reduction of atmospheric dinitrogen to ammonium
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
in absence of N2 or other substrates, the electron flow is directed towards proton reduction
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
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
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus PAL-5
-
-, biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii DJ1310
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae M5a1
-
-
-
-
ir
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
Chromatium sp., Rhizobium sp.
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
show the reaction diagram
-
mutant H195Q shows only about 7.5% activity compared to wild-type
-
?
reduced ferredoxin + H+ + SCN- + ATP
oxidized ferredoxin + H2S + HCN + ADP + phosphate
show the reaction diagram
-
-
-
?
Ti3+ + H+ + N2 + ATP
?
show the reaction diagram
-
in vitro substrate
-
-
?
methyl isocyanide + ?
?
show the reaction diagram
P00459
-
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
both nifI1 and nifI2 are required for regulation in vivo
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme performs acetylene reduction
-
-
-
additional information
?
-
-
enzyme activity causes acetylene production
-
-
-
additional information
?
-
-
nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
Azotobacter vinelandii DJ995
-
nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth, substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview
-
-
-
additional information
?
-
Klebsiella pneumoniae UN1217
-
substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
-
-
-
additional information
?
-
Gluconacetobacter diazotrophicus PAL-5
-
influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview
-
-
-
additional information
?
-
Azotobacter chroococcum YM68A
-
FeVco is extracted intact, carrying with it the characteristic capacity to reduce C2H2 to C2H6 and, perhaps even more importantly, the ability to reduce N2 to NH3
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Chromatium sp.
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter sp.
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Gloeocapsa sp.
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.
-
ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin, regulation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Cyanobacterium sp.
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
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
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azospirillum amazonense Y1
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Azotobacter vinelandii OP
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhizobium sp. ORS571
-
biological N2 fixation, ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Corynebacterium flavescens 301
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Rhodobacter capsulatus B10S
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
Escherichia coli C-M 74
-
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
-
the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3
-
-
?
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
P00459
enzyme complex is responsible for the majority of biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
-
reduction of atmospheric dinitrogen to ammonium
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Gluconacetobacter diazotrophicus PAL-5
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Azotobacter vinelandii DJ1310
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
show the reaction diagram
Klebsiella pneumoniae M5a1
-
-
-
-
ir
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
P00459
the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview
-
-
-
additional information
?
-
-
both nifI1 and nifI2 are required for regulation in vivo
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
enzyme activity causes acetylene production
-
-
-
additional information
?
-
-
nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor
-
-
-
additional information
?
-
Azotobacter vinelandii DJ995
-
nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth
-
-
-
additional information
?
-
Gluconacetobacter diazotrophicus PAL-5
-
influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
P00459
2 MgATP binding sites on the iron protein, binding changes the redox status of the [4Fe4S] cluster of the iron protein, mechanism, overview
ATP
-
the FeS cluster exhibits very little change upon MgATP binding
ATP
-
the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein
FeMo cofactor
-
-
-
FeMo cofactor
-
structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein
-
FeMo cofactor
-
bound at the active site, the MoFe protein, encoded by nifD and nifK. It is an alpha2beta2 heterotetramer with each nifD-encoded alpha subunit coordinating the FeMo cofactor that binds and reduces substrate, while alpha plus the nifK-encoded beta subunits coordinate the [8Fe-7S] P-cluster
-
FeMo cofactor
-
i.e. FeMoco cofactor, in the Mo-nitrogenase
-
FeMo cofactor
-
binding structure and mechanism, overview
-
FeMo cofactor
-
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview
-
FeMo protein
-
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
-
FeMo protein
-
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
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
iron cofactor
-
the Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein
-
iron-molybdenum cofactor
-
-
iron-molybdenum cofactor
-
dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the cofactor is composed of a [Mo-3Fe-3S] subcluster and a [4Fe3S] subcluster bridged by 3 sulfide pairs, with homocitrate bound to the molybdenum, structure determination and analysis
iron-molybdenum cofactor
-
enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, structure, redox status, part of the MoFe protein
iron-molybdenum cofactor
-
-
iron-molybdenum cofactor
-
required for activity of the enzyme complex, insertion in the presynthesized apodinitrogenase involving the monomeric 26 kDa NafY protein, which binds the FeMo cofactor with very high affinity via its HIs121, the cofactor-NafY-complex exhibits an EPR signal similar to isolated FeMo cofactor and the M-center of the enzyme, NafY also binds the biosynthetic precursor of the MoFe cofactor, the NifB-cofacor, determination of binding sites
iron-molybdenum cofactor
-
substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis
iron-molybdenum cofactor
-
molybdenum-iron protein component with an iron-molybdenum cofactor center, biosynthesis of the cofactor, detailed overview. NifS and NifU launch the process by synthesizing small Fe/S fragments, such as the [Fe2S2] clusters and the [Fe4S4] clusters. These small Fe/S building blocks are assembled into a large Fe/S core on NifB and further processed on NifEN with the assistance of Fe protein. Upon the completion of assembly on NifEN, the mature FeMoco is subsequently delivered to its target location within theMoFe protein, resulting in the formation of an active holo-MoFe protein
iron-molybdenum cofactor
-
located at the active site in the MoFe protein
iron-molybdenum cofactor
P07328
modelling of the FeMo-cofactor binding site in the alpha70Ile MoFe protein structure
iron-vanadium cofactor
-
i.e. FeVco cofactor, in the V-nitrogenase
-
additional information
-
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
-
additional information
-
structure of MoFe-cofactor
-
additional information
-
NifEN is a partially defective homologue of the MoFe protein, catalytic properties, overview. Components of the electron transfer chains in nitrogenase and its homologue, overview
-
additional information
-
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1.2 gatom per mol of MoFe protein
Co2+
-
divalent cation requirement is satisfied by Co2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Co2+
-
can replace Mg2+, but is less effective
Cu2+
-
1.4 gatom per mol of MoFe protein
Fe
-
molybdenum-iron protein component and an iron protein component with an iron-molybdenum cofactor center. Schematic structure of the alpha2-dimeric Fe protein, which contains a [Fe4S4] cluster at the subunit interface and an MgATP binding site within each subunit, overview
Fe
-
in the active site iron-molybdenum cofactor, and as 4Fe-4S cluster in the Fe protein
Fe2+
-
divalent cation requirement is satisfied by Fe2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Fe2+
-
can replace Mg2+, but is less effective
Fe2+
-
as part of the Fe protein in the MoFe protein, [4Fe-4S] clusters
Fe2+
-
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
Fe2+
-
different VO2+-nucleotide coordination environments exist for the Fe-protein Kp2 that depend on pH and are distinguishable by EPR spectroscopy, Kp2 structure, overview
Fe2+
-
in [Fe-S] clusters
Fe2+
-
part of the iron-molybdenum and molybdenum-iron cofactors
Fe2+
-
-
Iron
-
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
-
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
Iron
-
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
-
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
Iron
-
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
Iron
-
18-36 atoms of iron per molecule of MoFe protein , overview; iron content of the iron protein: 3.5
Iron
-
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
Iron
-
17.5 gatom per mol of MoFe protein; 4 atoms of iron per molecule of Fe protein
Iron
-
characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins
Iron
-
24 atoms of iron per molecule of MoFe protein
Iron
-
22.5 atoms of iron per molecule of protein; 3.1
Iron
-
4 atoms of iron per molecule of Fe protein
Iron
Azotobacter sp., Frankia sp., Gloeothece sp.
-
-
Iron
-
4 atoms of iron per molecule of Fe protein
Iron
Chromatium sp.
-
-
Iron
-
the iron-only enzyme consists of 2 components: Fe protein and FeFe protein, the latter contains 26 Fe atoms per molecul of protein
Iron
-
contains [4Fe4S] cluster; reduction kinetics
Iron
-
contains [4Fe4S] cluster
Iron
-
contains [4Fe4S] cluster
Iron
-
contains [4Fe4S] cluster
Iron
-
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
Iron
-
required, part of the MoFe protein cofactor
Iron
-
dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the enzyme complex contains also a dimeric iron protein
Iron
-
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
Iron
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
Iron
-
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
Iron
-
dependent on, the enzyme complex contains a molybdenum-iron protein, and a dimeric iron protein
Iron
-
enzyme contains an iron-molybdenum cofactor
Iron
-
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
Iron
-
component Gd1, iron and molybdenum in a 12:1 ratio. Component Gd2, 3.9 Fe atoms per molecule
Iron
P07328
in FeMo cofactor and MoFe protein
Iron
-
in the MoFe protein and the Fe protein
Iron
-
in the FeMo cofactor
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
-
1.8 gatom per mol of MoFe protein; Mg2+ required for MgATP complex
Mg2+
-
divalent metal requirement is satisfied by Mg2+, reaction is best supported by concentration of divalent cation one-half the concentration of ATP
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
Chromatium sp.
-
Mg2+ required for MgATP complex
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
-
Mg2+ required for MgATP complex
Mg2+
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
Mg2+
-
required, the FeS cluster exhibits very little change upon MgATP binding
Mg2+
-
MgATP2- is required
Mg2+
-
required
Mn2+
-
divalent cation requirement is satisfied by Mn2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Mn2+
-
can replace Mg2+, but is less effective
Mo
-
molybdenum-iron protein component with an iron-molybdenum cofactor center. Schematic structureof the alpha2beta2-tetrameric MoFe protein, which contains a pair of unique clusters in each ab-subunit dimer, the P-cluster ([Fe8S7]) at the alphabeta-subunit interface, and the FeMoco ([MoFe7S9X], where X=C,N, or O) within the alpha-subunit
Mo
-
in the active site iron-molybdenum cofactor
Molybdenum
-
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
-
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
Molybdenum
-
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
-
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
Molybdenum
-
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
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
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
Molybdenum
-
molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview; review on molybdenum in nitrogenase
Molybdenum
-
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
Molybdenum
-
review on molybdenum in nitrogenase
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
Molybdenum
-
1 gatom per mol of MoFe protein
Molybdenum
-
also possesses Mo-independent nitrogenases: one vanadium containing nitrogenase and another lacking both molybdenum and vanadium
Molybdenum
-
characterization of the metal clusters in the nitrogenase molybdenum-iron protein
Molybdenum
-
2 gatom per mol of MoFe protein
Molybdenum
-
1.2-1.3 gatom per mol of MoFe protein
Molybdenum
-
-
Molybdenum
Azotobacter sp., Frankia sp., Gloeothece sp.
-
-
Molybdenum
-
-
Molybdenum
-
23 mol Fe + 1.9 mol Mo per mol of MoFe protein
Molybdenum
-
molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview
Molybdenum
-
mol Mo per mol MoFeprotein: wild-type and mutant H195Q 1.9, mutant H195N and Q191K 0.9
Molybdenum
-
MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands
Molybdenum
-
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
Molybdenum
-
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
Molybdenum
-
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
Molybdenum
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
Molybdenum
-
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
Molybdenum
-
dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site
Molybdenum
-
enzyme contains an iron-molybdenum cofactor
Molybdenum
-
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
Molybdenum
-
component Gd1, iron and molybdenum in a 12:1 ratio, molybdenum content is 1.4 atoms per enzyme tetramer
Molybdenum
-
part of the iron-molybdenum and molybdenum-iron cofactors
Molybdenum
-
in the FeMoco cofactor of the MoFe protein
Molybdenum
P07328
in FeMo cofactor and MoFe protein
Molybdenum
-
in the MoFe protein
Ni2+
-
divalent cation requirement is satisfied by Ni2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Ni2+
-
can replace Mg2+, but is less effective
Tungsten
-
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
Vanadium
-
possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium
Vanadium
-
possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium
Vanadium
-
characterization of the metal clusters in the nitrogenase vanadium-iron protein
Vanadium
-
characterization of the metal clusters in the nitrogenase vanadium-iron protein
Vanadium
-
characterization of the metal clusters in the nitrogenase vanadium-iron protein
Vanadium
-
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
Vanadium
-
in the FeVco cofactor
Zn2+
-
0.8 gatom per mol of MoFe protein
Molybdenum
-
in the FeMo cofactor
additional information
-
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
additional information
-
-
additional information
-
-
additional information
Chromatium sp.
-
-
additional information
-
contains also an inactive MoFe protein species
additional information
-
-
additional information
-
the iron-only nitrogenase form contains no molybdenum, vanadium or any other heterometal atom
additional information
-
redox properties of metal clusters
additional information
-
structure and organization of metal clusters
additional information
-
structure and organization of metal clusters
additional information
-
rhenium cannot substitute for molybdenum in vitro, nor in vivo
additional information
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
additional information
-
structures of the metal centers in Fe protein and MoFe protein, overview
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,2-Dihydroxybenzene 3,5-disulfonate
-
-
2,3-Dimercaptopropanol
-
-
Acetylene
-
noncompetitive inhibition of N2 reduction
Acetylene
P00459
noncompetitive inhibition of nitrogen reduction, Gly69 is important
beryllium fluoride
P00459
inhibits by trapping of a stable Fe protein-MoFe protein nitrogenase complex
C2H2
-
inhibition of H195 mutants
C2H2
-
competitive to N2
CO
-
noncompetitive inhibitor of N2, C2H2 and N3- reduction, no inhibition of H+ reduction
CO
-
inhibition of CH4 and NH3 production from CN-
CO
-
inhibition of H+ reduction by about 50%
CO
-
binds to the active site
CO
P00459
strong inhibition, binding site and inhibition mechanism
cyanide
-
inhibits electron flow
H2
-
competitive inhibitor of N2, no inhibition of N3-, C2H2, CN- or H+ reduction
H2
-
competitive inhibition of N2 binding
hydrazine
-
and derivatives
L-asparagine
-
76% inhibition at 10 mM asparagine in the growth medium
L-aspartic acid
-
67% inhibition at 10 mM aspartic acid in the growth medium
L-cysteine
-
51% inhibition at 5 mM cysteine in the growth medium
L-Glutamic acid
-
68% inhibition at 10 mM glutamic acid in the growth medium
L-glutamine
-
60% inhibition at 10 mM glutamine in the growth medium
L-leucine
-
54% inhibition at 5 mM leucine in the growth medium
N2
-
inhibits C2H2 reduction of mutant H195Q; maximal inhibition of H2 production at Fe protein to MoFe protein ration 2.5
N2
-
inhibits the C2H2 reduction
N2
-
competitive inhibition of acetylene reduction
N2
-
inhibits hydrazine reduction
N3-
-
inhibits H2 production competitively and reversibly
NaCl
-
half-maximal inhibition at 100 mM
NAD+-malic enzyme
-
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
-
NH4+
-
immediate inhibition, repression of induction
NH4+
-
immediate inhibition, repression of induction
NH4+
-
18% inhibition at 5 mM, 32% at 15 mM ammonium in the growth medium
NH4Cl
-
nitrogenase activity is repressed by the addition of 0.5 mM NH4Cl
NIFI1,2
-
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
-
nitrate
-
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
-
NO3-
-
17% inhibition at 15 mM nitrate in the growth medium
O2
-
complete reversible inhibition, reversibility decreases by increasing the time of exposure to O2
O2
Cyanobacterium sp.
-
irreversibly inactivated
phosphate
-
above 30 mM
SCN-
-
above 6 mM occurs substrate inhibition
sodium nitroprusside
-
influence of the NO donor sodium nitroprusside on the relative levels of acetylene reduction activity, overview
tetrafluoroaluminate
P00459
inhibits by trapping of a stable Fe protein-MoFe protein nitrogenase complex, binds to the Fe protein
tungstate
-
30% inhibition at 0.01 mM, 50% inhibition at 0.1 mM, 95% inhibition at 1 mM, inhibits MoFe protein expression
Urea
-
immediate inhibition, repression of induction
Vanadium
-
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
VO2+
-
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
additional information
-
high ionic strength inhibits
-
additional information
-
e.g. above 50 mM NaCl; high ionic strength inhibits
-
additional information
-
enzyme activity and bacterial growth is affected by amino acids in the growth medium
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
C2H2
-
enhances the CH4 production but not NH3 production from CN-, wild-type enzyme
homocitrate
-
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
light
-
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
-
molybdate
-
induces MoFe protein expression
additional information
-
Fe protein contains an adenine-like molecule, a pentose moiety and a phosphate residue covalently attached to the molecule
-
additional information
-
Fe protein contains an adenine-like molecule, a pentose moiety and a phosphate residue covalently attached to the molecule
-
additional information
-
H2 generation activates N2 binding
-
additional information
-
several organic acids highly stimulate the enzyme activity of anaerobically isolated bacteroids, only malate has little effect
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
ATP
-
with C2H2
0.45
-
CH4
-
mutant H195Q
1.6
-
CH4
-
wild-type
4.5
-
CH4
-
mutant H195N
0.1
-
N2
-
with C2H2
12
-
CH4
-
mutant Q191K
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
overview, different substrates
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
EPR signals of Mo and of W containing cofactor, redox potentials
-
additional information
-
additional information
-
determination of EPR signals of wild-type enzyme and V70A mutant MoFe protein-containing enzyme with propargyl alcohol and C2H2 as substrates, temperature dependence
-
additional information
-
additional information
P00459
redox properties of metal clusters and P-cluster, overview
-
additional information
-
additional information
-
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
-
additional information
-
additional information
-
Km for N2 of wild-type and mutant enzyme
-
additional information
-
additional information
-
kinetic analysis, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
400
-
flavodoxin hydroquinone
-
before and after reduction of the nitrogenase complex relatively slow reactions take place, which limits the rate of the Fe protein cycle
-
additional information
-
additional information
-
1200 per min: proton production of the reduced enzyme, MgATP-dependent
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.024
-
-
purified mutant H195Q enzyme, anaerobic atmosphere
0.027
-
-
reductant dithionite, whole cell assay
0.066
-
-
crude extract, 100% Ar atmosphere, H2 production
0.13
-
-
V70I mutant, substrate acetylene, in presence of C2H4
0.17
-
-
V70I mutant, substrate N2, in presence of NH3
0.2
-
-
wild-type enzyme, substrate acetylene, in presence of H2
0.235
-
-
substrate N2, purified Mo nitrogenase
0.26
-
-
substrate C2H2, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1
0.27
-
-
mutant A175G, purified enzyme, substrate C2H2
0.35
-
-
substrate N2, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1
0.43
-
-
purified Fe protein
0.6
0.8
-
purified Fe protein
0.6
-
-
wild-type enzyme, substrate N2, in presence of NH3
0.64
-
-
wild-type enzyme, substrate N2, in presence of H2
0.7
-
-
purified MoFe protein
0.7
-
-
purified enzyme, anaerobic atmosphere
1.01
-
-
purified MoFe protein
1.07
-
-
purified MoFe protein
1.2
-
-
purified MoFe protein
1.2
-
-
substrate C2H2, purified Mo nitrogenase
1.26
-
-
purified Fe protein
1.3
-
-
substrate H+, purified Mo nitrogenase
1.5
1.7
-
purified MoFe protein
1.52
-
-
wild-type, purified enzyme, substrate C2H2
1.7
2.2
-
purified Fe protein
1.8
-
-
purified Fe protein
1.8
-
-
wild-type enzyme, substrate acetylene, in presence of C2H4
1.94
-
-
V70I mutant, substrate N2, in presence of H2
2
-
-
wild-type enzyme, C2H2 reduction
2
-
-
V70I mutant, substrate acetylene, in presence of H2
2.01
-
-
purified Fe protein
2.02
-
-
wild-type enzyme, substrate argon, in presence of H2
2.082
-
-
purified component II
2.16
-
-
purified component I
2.2
-
P07328
about, micromol/min/mg MoFe protein, mutant enzyme, pH not specified in the publication, temperature not specified in the publication
2.27
2.28
-
purified enzyme, substrate acetylene
2.316
-
P07328
about, micromol/min/mg MoFe protein, wild-type enzyme, pH not specified in the publication, temperature not specified in the publication
2.34
-
-
V70I mutant, substrate argon, in presence of H2
2.4
-
-
purified MoFe protein
2.4
-
-
substrate H+, iron-only nitrogenase with Fe protein to FeFe protein ratio of 40:1
additional information
-
-
activity of Fe proteins and MoFe proteins
additional information
-
-
-
additional information
-
-
activity of Fe proteins and MoFe proteins
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity of Fe proteins and MoFe proteins; overview
additional information
-
-
-
additional information
-
-
assay in anaerobic atmosphere required
additional information
-
-
assay in anaerobic atmosphere required; wild-type and diverse alpha-His195 MoFe protein mutants
additional information
-
-
in vivo activity measurement, quantification of ethylene
additional information
-
-
comparison of relative nitrogen-fixing ability, H2 production rates, and reduction rates of acetylene (under Ar) of wild-type and mutant NifD variants, overview
additional information
-
-
comparison of ATP consumption coupled to H2 production by recombinant NifDK/NifB-co and by NifDK, overview
additional information
-
-
rates of ATP hydrolysis by Mo and V nitrogenases are comparable under CO, which reflected a similar flux of electrons through the two nitrogenases
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
SCN- reduction
7
8
-
assay at, hydrazine reduction activity
7
-
-
assay at, N2 reduction activity
7.1
7.3
-
with substrates: N2, C2H2
7.4
-
-
assay at
7.5
-
-
assay at, acetylene reduction
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.3
-
pH 6.5: no activity below, pH 8.3: about 70% of activity maximum
6.5
8.5
-
below and above no remaining activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
40
-
no maximum with Ti3+ as reductant
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
in vivo assay at
30
-
-
assay at
additional information
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
40
-
no maximum with Ti3+ as reductant
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Cyanobacterium sp.
-
in heterocysteous cyanobacteria exclusive site of N2 fixation during aerobic growth
Manually annotated by BRENDA team
additional information
-
the enzyme is localized to the microaerobic environment of heterocysts, a highly differentiated subset of the filamentous cells
Manually annotated by BRENDA team
additional information
-
highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected, enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview
Manually annotated by BRENDA team
additional information
-
highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected 41C and above. Enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview
Manually annotated by BRENDA team
additional information
-
cultivated as symbiont in Lotus japonicus root nodules
Manually annotated by BRENDA team
additional information
Anabaena sp. PCC 7120
-
the enzyme is localized to the microaerobic environment of heterocysts, a highly differentiated subset of the filamentous cells
-
Manually annotated by BRENDA team
additional information
Crocosphaera watsonii WH8501
-
highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected, enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview
-
Manually annotated by BRENDA team
additional information
Gloeothece sp. PCC6909
-
highest nitrogenase activity is observed at 29C growth temperature. At 31C and above, nitrogenase activity is not detected 41C and above. Enzyme activity and acetylene production in relation to growth conditions, overview. Pattern of nitrogenase activity during the light-dark cycle, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
40000
-
Fe protein
40000
-
-
Fe protein, ultracentrifugation
44000
-
-
FeMo cofactor-NafY protein complex, gel filtration
46000
-
-
NafY protein, gel filtration, sedimentation equilibrium centrifugation
51000
-
-
Fe protein, gel filtration
56000
-
-
Fe protein, gel filtration
60000
-
Cyanobacterium sp.
-
Fe protein
61500
-
-
Fe protein
62000
-
-
Fe protein, gel filtration
63000
-
-
Fe protein
63000
-
-
Fe protein
63000
-
-
Fe protein
64000
-
-
Fe protein, gel filtration
64000
-
-
Fe protein, gel filtration
65000
-
-
Fe protein, gel filtration
66800
-
-
Fe protein
68200
-
-
Fe protein, ultracentrifugation
74000
-
-
Fe protein, gel filtration
160000
-
-
MoFe protein, estimation from Mo content, ultracentrifugation
168000
-
-
MoFe protein, ultracentrifugation
180000
-
-
MoFe protein, gel filtration
194000
-
-
MoFe protein, gel filtration
200000
250000
-
tungsten-substituted enzyme component, gel filtration
200000
-
-
MoFe protein, gel filtration
200000
-
-
MoFe protein, ultracentrifugation
200000
-
-
MoFe protein, ultracentrifugation
210000
-
-
MoFe protein, gel filtration
216000
-
-
MoFe protein, gel filtration
216000
-
Cyanobacterium sp.
-
nitrogenase complex
219000
-
-
MoFe protein, gel filtration
220000
-
-
MoFe protein, gel filtration
220000
-
-
MoFe protein, gel filtration
226000
-
-
MoFe protein, gel filtration
227000
-
-
MoFe protein, gel filtration
230000
-
-
MoFe protein
230000
-
-
MoFe protein
230000
-
-
MoFe protein
270000
-
-
MoFe protein, ultracentrifugation
additional information
-
-
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
additional information
-
-
-
additional information
-
-
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
additional information
-
-
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
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
comparison of amino acid composition
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
MoFe protein 4 * 60000 + Fe protein 2 * 30800, SDS-PAGE
?
-
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
?
-
component Gd1, subunits of 53000 and 57500 Da, component Gd2, subunits of 33000 Da, SDS-PAGE
?
Rhodobacter capsulatus B10S
-
FeFe protein of iron-only enzyme: 2 * 59000 + 2 * 51000 + 2 * 13500, alpha2beta2gamma2, SDS-PAGE; Fe protein of both enzyme forms: 2 * 30000-31000, gamma2, SDS-PAGE; MoFe protein: 2 * 59000 + 2 * 57000, alpha2beta2, SDS-PAGE
-
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 27500, SDS-PAGE
dimer
-
2 * 26141-28000, unassociated NafY protein, sequence calculation and sedimentation equilibrium centrifugation
dimer
-
2 * 26141-28000, unassociated NafY protein, sequence calculation and sedimentation equilibrium centrifugation
-
tetramer
-
MoFe protein is an alpha2beta2-tetramer
tetramer
-
alpha: 55000, beta: 59500; MoFe protein is an alpha2beta2-tetramer
tetramer
-
alpha: 58500, beta: 58500; MoFe protein is an alpha2beta2-tetramer
tetramer
-
-
tetramer
Cyanobacterium sp.
-
-
tetramer
-
alpha: 56000, beta: 59000
tetramer
-
component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE
tetramer
-
MoFe protein 1 * 55000 + 1 * 59000 + Fe protein 2 * 33500, SDS-PAGE
tetramer
-
tungsten-substituted enzyme component
tetramer
Corynebacterium flavescens 301, Escherichia coli C-M 74, Rhodobacter capsulatus B10S
-
-
-
dimer
Corynebacterium flavescens 301, Escherichia coli C-M 74
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
-
additional information
-
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
additional information
-
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
additional information
-
alpha-beta-monomer of the FeMo protein consists of the FeMo cofactor FeMo-co with the substrate reduction site and the [4Fe-4S] cluster
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
apo-MoFe protein has a alpha2beta2 subunit composition and interacts with Fe protein, can be rebuilt by addition of FeMo-cofactor
additional information
-
VFe protein form 1 has alphabeta2 conformation, VFe protein form 2 has alpha2beta2 conformation
additional information
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
additional information
-
the NafY protein monomerizes upon binding to the FeMo cofactor
additional information
-
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
additional information
-
Kp2 structure analysis bound to Vo2+, ATP, and ADP, characterization of the metal-nucleotide coordination environment, overview
additional information
-
Kp2 structure analysis bound to Vo2+ and at different pH, overview
additional information
-
components of the electron transfer chains in nitrogenase and its homologue, overview
additional information
Azospirillum amazonense Y1
-
-
-
additional information
-
the NafY protein monomerizes upon binding to the FeMo cofactor
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
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
additional information
-
posttranslational regulation of nitrogenase is mediated via GlnD, a bifunctional uridylyltransferase/uridylyl-removing enzyme which is important in nitrogen assimilation and metabolism
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure analysis of the iron protein, and of the MoFe protein
P00459
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
-
MoFe protein; purified enzyme is diluted at room temperature with 3 volumes of Tris-HCl 0.01 M, pH 7.2, immediate crystal formation
-
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
P07328
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
-
purified recombinant His-tagged NifH2, hanging drop vapour diffusion method, 0.001 l of 20 mg/ml protein in 2 mM Tris-HCl, pH 8.0, and 50 mM NaCl, is mixed with 0.001 ml of reservoir solution, containing 0.1 M sodium citrate, 8% PEG 8000, pH 5.0, and equilibrated against 0.15 ml of reservoir solution, 10 days, 4C, X-ray diffraction structure determination and analysis at 2.85 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
MoFe protein stable
8.7
-
-
50% loss of activity after overnight dialysis at pH 8.7
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
Fe protein, half-life: 18 h
additional information
-
-
Fe protein: cold labile
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nitrogenase complex is more stable than either the MoFe protein or the Fe protein alone
-
Fe protein is salt sensitive
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extreme sensitivity to O2
-
440142, 440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
440143
extreme sensitivity to O2
-
440144
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
stable to O2, no loss in nitrogen fixation activity
-
440148
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
extreme sensitivity to O2
-
440143, 440144
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
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
-
440158
extreme sensitivity to O2
-
440142, 440143, 440144
MoFe protein is extremely sensitive to O2
-
440147
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
440143
enzyme is extremely oxygen-labile
-
660287
extreme sensitivity to O2
-
440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
440143
extreme sensitivity to O2
-
440142, 440143, 440144
Fe protein is very O2 sensitive
-
440159
extreme sensitivity to O2
-
440144
extreme sensitivity to O2
Cyanobacterium sp.
-
440148
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
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
-
440140
extreme O2 lability, t1/2: 10 min, MoFe protein 45 s, Fe protein
-
440149
extreme sensitivity to O2
-
440142, 440143, 440144
MoFe protein is extremely sensitive to O2
-
440147
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
extreme sensitivity to O2
-
440143, 440144
extreme O2 lability, t1/2: 1 min, Fe protein
-
440165
extreme sensitivity to O2
-
440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
440143
overview: O2 lability and protection mechanisms against O2 in various organisms in vivo
-
440166
extreme sensitivity to O2
-
440142
extreme sensitivity to O2
-
440142, 440143, 440144
t1/2 Fe protein: 45 sec, t1/2 MoFe protein: 10 min
-
440143
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, anaerobic storage, overnight, complete loss of activity
-
0C, anaerobic conditions, FeMo protein stable
-
22C, O2-free atmosphere, pH 7-8, stable
-
5C, O2-free atmosphere, overnight, 80% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially, extraction of FeVco in an active form by N-methylformamide, and gel filtration of the reconstituted protein, overview
-
2 forms of VFe protein
-
FeMo-cofactorless MoFe protein from nifB deletion mutant
-
large scale; strict anaerobic conditions
-
mutant betaG69S
P00459
recombinant Azotobacter vinelandii NafY protein from Escherichia coli strain BL21(DE3)
-
recombinant wild-type Fe protein, recombinant His-tagged wild-type MoFe protein and recombinant His-tagged MoFe protein mutant V70A, to homogeneity
-
strict anaerobic conditions
-
wild-type and mutant H195Q
-
wild-type and mutants H195Q, H195N, Q191K
-
all components
-
strict anaerobic conditions
-
both components
-
native NifDK by gel filtration and affinity chromatography on a NifB resin, elution as NifDK/NifB-co complex
-
purification of the enzyme complex and isolation of the MoFe protein thereof
-
recombinant His-tagged NifH2 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration to over 95% purity
-
both components
-
iron-only nitrogenase, both components
-
molybdenum containing enzyme form, both components
-
wild-type and tungsten-substituted enzymes
-
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
-
amino acid sequence comparison with other species; expression in Escherichia coli, expression in Klebsiella pneumoniae, Anabaena gene library screening with genes of Klebsiella pneumoniae
-
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
-
expression of His-tagged wild-type and V70A mutant MoFe protein in strain DJ1310, expression of the wild-type Fe protein
-
genetic analysis
-
overexpression of Azotobacter vinelandii NafY protein in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
expression of nitrogenase in the absence of NH4+ and at initial O2 concentrations above 5% in the culture atmosphere
-
phylogenetic analysis, overview
-
gene MJ0685, expression of His-tagged NifH2 in Escherichia coli strain BL21 (DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F388 A
-
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
F388H
-
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
F388T
-
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
F388Y
-
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
H197A
-
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
H197D
-
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
H197E
-
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
H197F
-
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
H197G
-
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
H197K
-
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
H197L
-
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
H197N
-
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
H197Q
-
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
H197R
-
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
H197S
-
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
H197T
-
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
Q193A
-
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
Q193G
-
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
Q193H
-
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
Q193K
-
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
Q193L
-
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
Q193N
-
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
Q193S
-
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
Q193V
-
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
R284C
-
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
R284E
-
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
R284F
-
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
R284H
-
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
R284K
-
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
R284L
-
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
R284Q
-
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
R284T
-
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
R284Y
-
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
S285A
-
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
S285C
-
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
S285D
-
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
S285G
-
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
S285M
-
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
S285N
-
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
S285Q
-
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
S285T
-
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
Y236A
-
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
Y236D
-
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
Y236F
-
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
Y236H
-
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
Y236M
-
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
Y236N
-
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
Y236T
-
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
H197A
Anabaena sp. PCC 7120
-
site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
-
H197N
Anabaena sp. PCC 7120
-
site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
-
A175G
-
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
A175S
-
unable to support substrate reduction because of an inability to undergo a required MgATP-induced conformational change
D125E
P00459
site-directed mutagenesis, mutation alters the properties of the MgATP2- binding site with bound MgADP
G69S
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
H195G
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, slightly decreased Fe protein activity, altered phenotype
H195L
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, increased Fe protein activity, altered phenotype
H195N
-
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
H195N
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, altered phenotype
H195Q
-
alphaHis195 of MoFe protein, shows 159% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition
H195Q
-
below 2% N2 reducing activity remaining compared to wild-type due to less effective N2 binding
H195Q
-
alpha-His of MoFe protein, site directed mutagenesis, decreased MoFe protein activity, altered phenotype
H195T
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype
H195Y
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype
Q191A/V70A
-
site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene
Q191K
-
alphaGln191 of MoFe protein, shows 6% activity compared to wild-type, substrate CN-, not affected by addition of C2H2
S188C
P00459
site-directed mutagenesis, mutation of a residue within the P-cluster of the beta-subunit, alters the EPR signal of the MoFe protein
S69G
-
alpha-subunit MoFe protein, resistant to inhibition by C2H2, thus acetylene binding/reduction site is not directly relevant to the mechanism of nitrogen reduction
V70A
-
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
V70A
-
site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme
V70A
-
site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne
V70A/H195Q
-
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
V70G
-
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
V70I
-
site-directed mutagenesis, decreased the hydrazine reduction activity
V70I
-
site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene
V70I
-
the mutant is suitable for analysis of reaction intermediates, since it exhibits the highest concentration of trapped H+-intermediate when turned over under Ar
V70I
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
V70X
-
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
H197Y
-
site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
additional information
-
engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview
H197T
Anabaena sp. PCC 7120
-
site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
-
additional information
Anabaena sp. PCC 7120
-
engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview
-
R284Q
Anabaena sp. PCC 7120
-
site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
-
additional information
-
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
K15Q
P00459
site-directed mutagenesis, mutation inhibits the communication of the [4Fe4S] cluster with the MgATP2- binding site
additional information
-
construction of mutant strain RP114
additional information
-
natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster
additional information
-
-
additional information
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
additional information
-
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
additional information
-
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
additional information
-
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
additional information
-
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
V70A
Azotobacter vinelandii DJ1310
-
site-directed mutagenesis of an alpha subunit residue of the MoFe cofactor, mutation alters the active site structure, trapping of propargyl alcohol at the active site for structure analysis
-
additional information
-
transposon insertion mutants of several plasmids
additional information
-
strains mutated in the nifX or orf1 genes show 90% or 50% reduction in nitrogenase activity under low levels of iron or molybdenum, respectively
additional information
-
generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
additional information
Klebsiella pneumoniae UN1217
-
generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
-
additional information
-
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
additional information
Rhodobacter capsulatus B10S
-
construction of 2 mutants strain: 1 kanamycin-resistant with a deletion in NifHDK and 1 kanamycin, gentamycin, and molybdenum-resistant with double deletion in nif HDK and modABCD
-
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme is reconstituted from N-methylformamide extraction
-
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
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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
energy production
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the reaction produces H2 as a by-product and is interesting for production of clean energy