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Information on EC 1.19.6.1 - nitrogenase (flavodoxin)
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1.19.6.1 nitrogenase (flavodoxin)IUBMB Comments
Requires Mg2+. It is composed of two components, dinitrogen reductase and dinitrogenase, that can be separated but are both required for nitrogenase activity. Dinitrogen reductase is a [4Fe-4S] protein, which, at the expense of ATP, transfers electrons from a dedicated flavodoxin to dinitrogenase. Dinitrogenase is a protein complex that contains either a molybdenum-iron cofactor, a vanadium-iron cofactor, or an iron-iron cofactor, that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia. The reduction is initiated by formation of hydrogen. The enzyme can also reduce acetylene 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. Some enzymes utilize ferredoxin rather than flavodoxin as the electron donor (see EC 1.18.6.1, nitrogenase).
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Word Map
- 1.19.6.1
- azotobacter
- vinelandii
- mgadp
-
mofe-protein
-
molybdenum-iron
- nifu
-
rhodospirillum
- dinitrogenase
-
femo-cofactor
- pasteurianum
-
mgadp-bound
- bacteriochlorophyll
-
nucleotide-bound
- nitrogenases
-
dark-operative
-
nucleotide-induced
- protochlorophyllide
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
4
+
2
+
+
16
+
16
=
4
+
2
+
+
16
+
16
Synonyms
nitrogenase fe protein, nitrogenase fe-protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nitrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
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
-
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
mechanism, Fe protein cycle
-
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
enzyme complex dissociation and association kinetics
-
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
residues Asn11, Ser68, and Asn72 of the flavodoxin are involved in complex formation between the flavodoxin and the Fe protein of the enzyme, influenced by MgADP-
-
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
reaction mechanism, overview
-
4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
reduced flavodoxin:dinitrogen oxidoreductase (ATP-hydrolysing)
Requires Mg2+. It is composed of two components, dinitrogen reductase and dinitrogenase, that can be separated but are both required for nitrogenase activity. Dinitrogen reductase is a [4Fe-4S] protein, which, at the expense of ATP, transfers electrons from a dedicated flavodoxin to dinitrogenase. Dinitrogenase is a protein complex that contains either a molybdenum-iron cofactor, a vanadium-iron cofactor, or an iron-iron cofactor, that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia. The reduction is initiated by formation of hydrogen. The enzyme can also reduce acetylene 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. Some enzymes utilize ferredoxin rather than flavodoxin as the electron donor (see EC 1.18.6.1, nitrogenase).
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CAS REGISTRY NUMBER
COMMENTARY
9013-04-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
reduced flavodoxin + H+ + acetylene + ATP
oxidized flavodoxin + ethylene + ADP + phosphate
-
-
-
-
?
reduced flavodoxin + N2 + ATP + H2O
oxidized flavodoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced flavodoxin II + N2 + ATP + H2O
oxidized flavodoxin II + H2 + NH3 + ADP + phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is not essential but required for maximum in vivo nitrogenase activity
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
enzyme consists of 2 metalloproteins, Fe protein and MoFe protein, which 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
i.e. flavodoxin semiquinone
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin reduces the Fe protein of the enzyme
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
slow enzyme
i.e. flavodoxin semiquinone
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is encoded by nifF gene, pyruvate:flavodoxin oxidoreductase by nifJ gene
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
intermediate is a flavodoxin hydroquinone
i.e. flavodoxin semiquinone
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
enzyme consists of 2 metalloproteins, Fe protein and MoFe protein, which 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
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
analysis of active sites for N2 and H+ reduction on FeMo-cofactor of nitrogenase
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is not essential but required for maximum in vivo nitrogenase activity
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin reduces the Fe protein of the enzyme
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is encoded by nifF gene, pyruvate:flavodoxin oxidoreductase by nifJ gene
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin reduces the Fe protein of the enzyme
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
highly specific for flavodoxin as electron donor
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
slow enzyme
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is encoded by nifF gene, pyruvate:flavodoxin oxidoreductase by nifJ gene
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is encoded by nifF gene, pyruvate:flavodoxin oxidoreductase by nifJ gene
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
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, not ferredoxin is effective in coupling electron flow to nitrogenase
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
anaerobic conditions are required by the enzyme
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
flavodoxin is encoded by nifF gene, pyruvate:flavodoxin oxidoreductase by nifJ gene
-
?
N2H2 + H+
NH3
-
diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, cofactor binding structure and kinetic mechanism, overview
-
-
?
N2H2 + H+
NH3
-
diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, cofactor binding structure and kinetic mechanism, overview
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
nitrogenase catalyzes the sequential addition of six electrons and six protons to a N2 that is bound to the active site metal cluster FeMo-cofactor, yielding two ammonia molecules
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
nitrogenase catalyzes the sequential addition of six electrons and six protons to a N2 that is bound to the active site metal cluster FeMo-cofactor, yielding two ammonia molecules
-
-
?
additional information
?
-
-
dithionite can serve as reductant in vitro
-
-
?
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
?
-
-
diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, hydrazine in reduced in absence of H2. Diazene joins the normal N2-reduction pathway, and diazene- and hydrazine-trapped turnover states represent the same intermediate in the normal reduction of N2 by nitrogenase, implications for the N2 reductionmechanism, overview
-
-
?
additional information
?
-
-
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
?
-
-
diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, hydrazine in reduced in absence of H2. Diazene joins the normal N2-reduction pathway, and diazene- and hydrazine-trapped turnover states represent the same intermediate in the normal reduction of N2 by nitrogenase, implications for the N2 reductionmechanism, overview
-
-
?
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
?
-
-
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
?
-
-
sodium dithionite and reduced methyl viologen can in vitro reduce the flavodoxin and the enzyme directly
-
-
?
additional information
?
-
-
see EC 1.18.6.1, from the literature for the enzymes EC 1.19.6.1 and EC 1.18.6.1 it is not obvious whether they are in fact to different enzymes
-
-
?
additional information
?
-
-
both nifI1 and nifI2 are required for regulation in vivo
-
-
?
additional information
?
-
-
the enzyme performs acetylene reduction
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
reduced flavodoxin + N2 + ATP + H2O
oxidized flavodoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced flavodoxin II + N2 + ATP + H2O
oxidized flavodoxin II + H2 + NH3 + ADP + phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
enzyme consists of 2 metalloproteins, Fe protein and MoFe protein, which 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
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
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, not ferredoxin is effective in coupling electron flow to nitrogenase
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
anaerobic conditions are required by the enzyme
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
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
?
-
-
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
?
-
-
both nifI1 and nifI2 are required for regulation in vivo
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
MoFe protein
-
two parallel electron channels may exist between the [8Fe-7S] cluster and FeMo-cofactor
-
ATP
-
the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites
FeMo cofactor
-
structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Mg2+
Molybdenum
Fe2+
-
as part of the Fe protein in the MoFe protein, [8Fe-7S] clusters
Fe2+
-
in the the active site metal cluster FeMo-cofactor, the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites
Fe2+
-
as part of the Fe protein in the MoFe protein, [4Fe-4S] clusters
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 contains an [Fe4S4] cluster that is in vivo reduced to the all-ferrous oxidation state[Fe4S4]0 and to a spin state S = 0 by flavodoxin hydroquinone
Mg2+
-
the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide suppresses the inhibition by nitrate
O2
-
complete reversible inhibition, reversibility decreases by increasing the time of exposure to O2
sodium nitroprusside
-
inhibits acetylene-reduction activity of nitrogenase by 1 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state turnover analysis with diazene and hydrazine bound to the FeMo cofactor, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
400
flavodoxin hydroquinone
-
before and after reduction of the nitrogenase complex relative slow reactions take place, which limits the rate of the Fe protein cycle
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
H+ and N2 reduction activities of wild-type and mutant Azotobacter vinelandii strains under 100% N2, overview
additional information
-
coupled assay with pyruvate:flavodoxin oxidoreductase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G6F558_LACDE
148
0
16397
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
alpha-beta-monomer of the FeMo protein consists of the FeMo cofactor FeMoco with the substrate reduction site and the P-cluster
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
-
the Mo-based nitrogenase is composed of two component proteins called the Fe protein and the MoFe protein
additional information
-
the Mo-based nitrogenase is composed of two component proteins called the Fe protein and the MoFe protein
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.17 A resolution. The structure displays typical structural motifs shared by other nitrogen-fixaion flavodoxins, a leucine at the re face of the isoalloxazine, an eight-residue insertion at the C-terminus of the 50s loop and a remarkable difference in the electrostatic potential surface with respect to non-nitrogenfixation flavodoxins
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alphaH195Q
-
site-directed mutagenesis, the mutant shows an altered electron transfer substrate specificity compared to the wild-type enzyme,overview
alphaQ191K
-
site-directed mutagenesis, the mutant shows reduced electron transfer activity compared to the wild-type enzyme, it reduces only H+, not N2, overview
Q191A/V70A
-
site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene
V70A
-
site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne
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, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene
Q191A/V70A
-
site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene
-
V70A
-
site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne
-
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, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene
-
additional information
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
-
construction of Qalpha191K, Halpha195Q, nifValpha, Qalpha191K/nifValpha and Halpha195Q/nifValpha mutants and determination of their substrate specificity, the mutant strains all show reduced electron transfer, overview
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
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
nitrogenase activity decline due to salinity stress is significantly lower and delayed in plants nodulated by flavodoxin-expressing bacteria than after nodulation by wild-type bacteria. After 3 days of stress, this decrease is approximately 60% for nodules elicited by wild-type bacteria and only 40% for flavodoxin-expressing nodules. Overexpression of flavodoxin in bacteroids has a protective effect on the function and structure of alfalfa nodules subjected to salinity stress conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haaker, H.; Klugkist, J.
The bioenergetics of electron transport to nitrogenase
FEMS Microbiol. Rev.
46
57-71
1987
Klebsiella pneumoniae
-
brenda
Yoch, D.C.
Electron transport carriers involved in nitrogen fixation by the coliform, Klebsiella pneumoniae
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83
153-164
1974
Klebsiella pneumoniae
brenda
Shah, V.K.; Stacey, G.; Brill, W.J.
Electron transport to nitrogenase. Purification and characterization of pyruvate:flavodoxin oxidoreductase. The nifJ gene product
J. Biol. Chem.
258
12064-12068
1983
Klebsiella pneumoniae
brenda
Bennett, L.T.; Jacobson, M.R.; Dean, D.R.
Isolation, sequencing, and mutagenesis of the nifF gene encoding flavodoxin from Azotobacter vinelandii
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263
1364-1369
1988
Azotobacter vinelandii, Azotobacter vinelandii OP
brenda
Duyvis, M.G.; Wassink, H.; Haaker, H.
Nitrogenase of Azotobacter vinelandii: kinetic analysis of the Fe protein redox cycle
Biochemistry
37
17345-17354
1998
Azotobacter vinelandii
brenda
Peelen, S.; Wijmenga, S.; Erbel, P.J.; Robson, R.L.; Eady, R.R.; Vervoort, J.
Possible role of a short extra loop of the long-chain flavodoxin from Azotobacter chroococcum in electron transfer to nitrogenase: complete 1H, 15N and 13C backbone assignments and secondary solution structure of the flavodoxin
J. Biomol. NMR
7
315-330
1996
Azotobacter chroococcum
brenda
Kavanagh, E.P.; Hill, S.
Oxygen inhibition of nitrogenase activity in Klebsiella pneumoniae
J. Gen. Microbiol.
139
1307-1314
1992
Klebsiella pneumoniae
brenda
Yakunin, A.F.; Gennaro, G.; Hallenbeck, P.C.
Purification and properties of a nif-specific flavodoxin from the photosynthetic bacterium Rhodobacter capsulatus
J. Bacteriol.
175
6775-6780
1993
Rhodobacter capsulatus
brenda
Lowery, T.J.; Wilson, P.E.; Zhang, B.; Bunker, J.; Harrison, R.G.; Nyborg, A.C.; Thiriot, D.; Watt, G.D.
Flavodoxin hydroquinone reduces Azotobacter vinelandii Fe protein to the all-ferrous redox state with a S = 0 spin state
Proc. Natl. Acad. Sci. USA
103
17131-17136
2006
Azotobacter vinelandii
brenda
Dodsworth, J.A.; Leigh, J.A.
NIFI1,2 inhibits nitrogenase by competing with Fe protein for binding to the MoFe protein
Biochem. Biophys. Res. Commun.
364
378-382
2007
Methanococcus maripaludis
brenda
Barney, B.M.; McClead, J.; Lukoyanov, D.; Laryukhin, M.; Yang, T.C.; Dean, D.R.; Hoffman, B.M.; Seefeldt, L.C.
Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reduction
Biochemistry
46
6784-6794
2007
Azotobacter vinelandii, Azotobacter vinelandii DJ995
brenda
Guan, F.; Zhao, D.; Pan, M.; Jiang, W.; Li, J.
Analysis of active sites for N2 and H+ reduction on FeMo-cofactor of nitrogenase
Chin. Sci. Bull.
52
2088-2094
2007
Azotobacter vinelandii
-
brenda
Dos Santos, P.C.; Mayer, S.M.; Barney, B.M.; Seefeldt, L.C.; Dean, D.R.
Alkyne substrate interaction within the nitrogenase MoFe protein
J. Inorg. Biochem.
101
1642-1648
2007
Azotobacter vinelandii, Azotobacter vinelandii DJ995
brenda
Kato, K.; Kanahama, K.; Kanayama, Y.
Involvement of nitric oxide in the inhibition of nitrogenase activity by nitrate in Lotus root nodules
J. Plant Physiol.
167
238-241
2010
Lotus japonicus
brenda
Perez-Dorado, I.; Bortolotti, A.; Cortez, N.; Hermoso, J.A.
Structural and phylogenetic analysis of Rhodobacter capsulatus NifF: uncovering general features of nitrogen-fixation (nif)-flavodoxins
Int. J. Mol. Sci.
14
1152-1163
2013
Rhodobacter capsulatus
brenda
Redondo, F.J.; Coba de la Pena, T.; Lucas, M.M.; Pueyo, J.J.
Alfalfa nodules elicited by a flavodoxin-overexpressing Ensifer meliloti strain display nitrogen-fixing activity with enhanced tolerance to salinity stress
Planta
236
1687-1700
2012
Medicago sativa
brenda
Pence, N.; Tokmina-Lukaszewska, M.; Yang, Z.Y.; Ledbetter, R.N.; Seefeldt, L.C.; Bothner, B.; Peters, J.W.
Unraveling the interactions of the physiological reductant flavodoxin with the different conformations of the Fe protein in the nitrogenase cycle
J. Biol. Chem.
292
15661-15669
2017
Azotobacter vinelandii
brenda
Segal, H.M.; Spatzal, T.; Hill, M.G.; Udit, A.K.; Rees, D.C.
Electrochemical and structural characterization of Azotobacter vinelandii flavodoxin II
Protein Sci.
26
1984-1993
2017
Azotobacter vinelandii
brenda
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