Any feedback?
Information on EC 1.7.7.1 - ferredoxin-nitrite reductase
for references in articles please use BRENDA:EC1.7.7.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.7.7.1 ferredoxin-nitrite reductaseIUBMB Comments
An iron protein. Contains siroheme and [4Fe-4S] clusters.
Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ferredoxin-nitrite reductase, assimilatory nitrite reductase, ferredoxin:nitrite reductase, ferredoxin:nitrite oxidoreductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
assimilatory NiR
CYME_CMG021C
CYME_CMJ117C
NiR
nitrite reductase
reductase, ferredoxin-nitrite
-
-
-
-
SiRA
SirB
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
sequential reaction scheme
-
NH3 + 2 H2O + 3 oxidized ferredoxin = nitrite + 3 reduced ferredoxin + 7 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ammonia:ferredoxin oxidoreductase
An iron protein. Contains siroheme and [4Fe-4S] clusters.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37256-44-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
hydroxylamine + reduced ferredoxin
ammonia + H2O + oxidized ferredoxin
hydroxylamine can serve as an electron-accepting substrate for the enzyme and the product of hydroxylamine reduction is ammonia. Hydroxylamine, bound to the enzyme, can serve as a late intermediate during the reduction of nitrite to ammonia catalyzed by the enzyme
-
-
?
hydroxylamine + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced 2,6-dichlorophenolindophenol
NH3 + oxidized 2,6-dichlorophenolindophenol + H2O
-
less than 35% of maximum activity compared to reduced methyl viologen as electron donor
-
-
?
nitrite + reduced phenazine methosulphate
NH3 + oxidized phenazine methosulphate + H2O
-
less than 35% of maximum activity compared to reduced methyl viologen as electron donor
-
-
?
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
nitrite + 6 reduced Fdx2
ammonia + 2 H2O + 6 oxidized Fdx2
-
Fdx2 i.e. Chlamydomonas reinhardtii plant-type isoform ferredoxin 2. Fdx2 is a more specific electron donor to NiR than ferredoxin
-
-
?
nitrite + 6 reduced Fdx2
ammonia + 2 H2O + 6 oxidized Fdx2
Fdx2 i.e. Chlamydomonas reinhardtii plant-type isoform ferredoxin 2
-
-
?
nitrite + 6 reduced ferredoxin
ammonia + 2 H2O + 6 oxidized ferredoxin
-
-
-
-
?
nitrite + 6 reduced ferredoxin
ammonia + 2 H2O + 6 oxidized ferredoxin
-
-
-
-
?
nitrite + 6 reduced ferredoxin
ammonia + 2 H2O + 6 oxidized ferredoxin
-
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
-
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
assimilatory nitrite reductase
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
ferredoxin is almost as efficient as methyl viologen as electron donor
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
assimilatory nitrite reductase
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
ferredoxin is almost as efficient as methyl viologen as electron donor
-
-
?
nitrite + FADH2
NH3 + FAD + H2O
-
50% of maximum activity compared to reduced methyl viologen as electron donor
-
-
?
nitrite + FADH2
NH3 + FAD + H2O
-
50% of maximum activity compared to reduced methyl viologen as electron donor
-
-
?
nitrite + NADPH + H+
NH3 + NADP+ + H2O
-
10% of maximum activity compared to reduced methyl viologen as electron donor
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
enzyme forms a covalent adduct with ferredoxin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: benzyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donors: flavodoxin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
enzyme can also catalyze the reduction of hydroxylamine to ammonia, at lower rate
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
NADPH
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donors: flavodoxin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
enzyme can also catalyze the reduction of hydroxylamine to ammonia, at lower rate
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
methyl viologen can serve as a less effective electron donor
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
NADPH
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donors: flavodoxin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
not: flavin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: benzyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
electrostatic interactions between ferredoxin and nitrite reductase play an important role in the reaction mechanism
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donors: flavodoxin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
enzyme can also catalyze the reduction of hydroxylamine to ammonia, at lower rate
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
methyl viologen can serve as a less effective electron donor
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second step of nitrate assimilation
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donor: methyl viologen
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
other electron donors: flavodoxin
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
enzyme can also catalyze the reduction of hydroxylamine to ammonia, at lower rate
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
NADH or NADPH can not serve as electron donors
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second step of nitrate assimilation
-
-
?
nitrite + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
a severe suppression of nitrite reductase by antisense technology drastically reduces the growth and development of transformed tobacco plants
-
-
?
nitrite + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
electrons from ferredoxin are first transferred to the [4Fe-4S] cluster, then to the siroheme and finally to the substrate
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
ferredoxin is almost as efficient as methyl viologen as electron donor
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
ferredoxin is almost as efficient as methyl viologen as electron donor
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl viologen
-
-
-
-
?
additional information
?
-
presence of two separate one-electron redox couples with Em values of -255 mV and -390 mV, respcetively
-
-
?
additional information
?
-
enzyme additionally shows activity of sulfite reductase, EC 1.8.7.1
-
-
?
additional information
?
-
enzyme additionally shows activity of sulfite reductase, EC 1.8.7.1
-
-
?
additional information
?
-
enzyme additionally shows activity of sulfite reductase, EC 1.8.7.1
-
-
?
additional information
?
-
-
no activity with NADH as electron donor
-
-
?
additional information
?
-
-
no activity with NADH as electron donor
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
-
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
assimilatory nitrite reductase
-
-
?
nitrite + 6 reduced ferredoxin + 7 H+
NH3 + 2 H2O + 6 oxidized ferredoxin
-
assimilatory nitrite reductase
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second step of nitrate assimilation
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second step of nitrate assimilation
-
-
?
nitrite + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
a severe suppression of nitrite reductase by antisense technology drastically reduces the growth and development of transformed tobacco plants
-
-
?
nitrite + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Iron
Iron
-
contains about 2 mol of siroheme per mol of enzyme, 3 mol of iron per mol of enzyme (MW 61000), one in siroheme, one (Fe2-S2)
Iron
-
4.8 Fe atoms per molecule of MW 63000, 0.93 mol siroheme per mol of enzyme
Iron
-
enzyme contains 1 tetranuclear center (4Fe-4S) and 1 siroheme, minimum of 5 Fe atoms per active enzyme molecule
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal-5'-phosphate
75% inhibition of the enzyme with ferredoxin as electron donor after exposure to NaBH4, but no inhibition of the enzyme with methyl viologen as electron donor
N-acetylsuccinimide
specifically inhibits the ferredoxin binding ability of the enzyme by modifying lysine residues
N-acetylsuccinimide
-
loss of enzymatic activity when reduced ferredoxin serves as electron donor, but very little effect with methyl viologen as electron donor, ferredoxin protects the enzyme
N-bromosuccinimide
-
incubation for 8 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity without effect on substrate binding or other enzyme activities, complex formation with ferredoxin protects the enzyme against inhibition
N-bromosuccinimide
-
incubation for 8 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity without effect on substrate binding or other enzyme activities, complex formation with ferredoxin protects the enzyme against inhibition; modifies tryptophane and cysteine residues, incubation for 8 hours with 8-fold excess of NBS leads to 50% inhibition of the catalytic activity, incubation for 16 hours with 8-fold excess of NBS leads to 80% inhibition of the catalytic activity
p-hydroxymercuribenzoate
-
enzyme from higher plants and eukaryotic algae inhibited, cyanobacterial enzyme not
p-hydroxymercuribenzoate
-
enzyme from higher plants and eukaryotic algae inhibited, cyanobacterial enzyme not
p-hydroxymercuribenzoate
-
enzyme from higher plants and eukaryotic algae inhibited, cyanobacterial enzyme not