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Information on EC 1.7.7.1 - ferredoxin-nitrite reductase and Organism(s) Spinacia oleracea and UniProt Accession P05314
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1.7.7.1 ferredoxin-nitrite reductaseIUBMB Comments
An iron protein. Contains siroheme and [4Fe-4S] clusters.
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The taxonomic range for the selected organisms is: Spinacia oleracea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ferredoxin-nitrite reductase, assimilatory nitrite reductase, ferredoxin:nitrite reductase, ferredoxin:nitrite oxidoreductase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
reductase, ferredoxin-nitrite
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NH3 + 2 H2O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H+
mechanism
-
NH3 + 2 H2O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H+
sequential reaction scheme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
ammonia:ferredoxin oxidoreductase
An iron protein. Contains siroheme and [4Fe-4S] clusters.
CAS REGISTRY NUMBER
COMMENTARY
37256-44-3
-
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
NH3 + H2O + oxidized ferredoxin
-
-
-
-
?
NH3 + H2O + oxidized ferredoxin
nitrite + reduced ferredoxin + H+
-
-
-
-
r
nitrite + reduced methyl viologen
NH3 + H2O + oxidized methyl 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
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-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
methyl viologen can serve as a less effective electron donor
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-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
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-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second step of nitrate assimilation
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-
?
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
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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
nitrite + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second enzyme of photosynthetic nitrate-reducing system
-
-
?
nitrite + reduced ferredoxin
ammonia + oxidized ferredoxin
-
second step of nitrate assimilation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-acetylsuccinimide
specifically inhibits the ferredoxin binding ability of the enzyme by modifying lysine residues
Phenylglyoxal
inhibits the ability of the enzyme to form a high-affinity complex with ferredoxin by modifying arginine residues
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
-
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
p-hydroxymercuribenzoate
-
enzyme from higher plants and eukaryotic algae inhibited, cyanobacterial enzyme not
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
-
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
Phenylglyoxal
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover number decreases about 20% after treatment with N-bromosuccinimide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 8.3
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pH 6.8: about 75% of activity maximum, pH 8.3: about 70% of activity maximum
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). NIR_SPIOL
594
0
66394
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000 - 63000
63000
additional information
additional information
-
the native enzyme with a MW of 85000 can be split into a modified form of a MW of 61000 that retains activity with the non-physiological electron-donor, methyl viologen but loses most of the ferredoxin-linked activity and an 24000 MW coupling protein fragment in which the ferredoxin-binding domain is located
additional information
-
the native enzyme with a MW of 85000 can be split into a modified form of a MW of 61000 that retains activity with the non-physiological electron-donor, methyl viologen but loses most of the ferredoxin-linked activity and an 24000 MW coupling protein fragment in which the ferredoxin-binding domain is located
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
spinach: the native enzyme with a molecular weight of 85000 can be split into a modified form with a MW of 61000 that retains activity with the non-physiological electron-donor methyl viologen, but loses most of the ferredoxin-linked activity and an 24000 MW coupling protein fragment in which the ferredoxin-binding domain is located
additional information
-
spinach: the native enzyme with a molecular weight of 85000 can be split into a modified form with a MW of 61000 that retains activity with the non-physiological electron-donor methyl viologen, but loses most of the ferredoxin-linked activity and an 24000 MW coupling protein fragment in which the ferredoxin-binding domain is located
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repetitive freezing and thawing or prolonged dialysis produces a loss of enzyme activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
-
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guerrero, M.G.; Vega, J.M.; Losada, M.
The assimilatory nitrate-reducing system and its regulation
Annu. Rev. Plant Physiol.
32
169-204
1981
Cucurbita pepo, Neopyropia yezoensis, Spinacia oleracea, Synechococcus elongatus PCC 7942 = FACHB-805, [Chlorella] fusca
-
Mikami, B.; Ida, S.
Spinach ferredoxin-nitrite reductase: characterization of catalytic activity and interaction of the enzyme with substrates
J. Biochem.
105
47-50
1989
Spinacia oleracea
Back, E.; Burkhart, W.; Moyer, M.; Privalle, L.; Rothstein, S.
Isolation of cDNA clones coding for spinach nitrite reductase: complete sequence and nitrate induction
Mol. Gen. Genet.
212
20-26
1988
Spinacia oleracea
Vega, J.M.; Cardenas, J.; Losada, M.
Ferredoxin-nitrite reductase
Methods Enzymol.
69
255-270
1980
Anabaena cylindrica, Cucurbita pepo, Dunaliella tertiolecta, Spinacia oleracea, Synechococcus elongatus PCC 7942 = FACHB-805, [Chlorella] fusca
-
Ida, S.; Mikami, B.
Spinach ferredoxin-nitrite reductase: a purification procedure and characterization of chemical properties
Biochim. Biophys. Acta
871
167-176
1986
Spinacia oleracea
-
Stein Privalle, L.; Privalle, C.T.; Leonardy, N.J.; Kamin, H.
Interactions between spinach ferredoxin-nitrite reductase and its substrates. Evidence for the specificity of ferredoxin
J. Biol. Chem.
260
14344-14350
1985
Spinacia oleracea
Ishiyama, Y.; Shinoda, I.; Fukushima, K.; Tamura, G.
Immunological comparison of nitrite reductase from different plant sources
Agric. Biol. Chem.
49
2225-2226
1985
Allium tuberosum, Arthrospira platensis, Hordeum vulgare, Phaseolus vulgaris, Spinacia oleracea, Symphytum officinale, Vigna angularis, Zea mays
-
Hirasawa, M.; Tamura, G.
Purification of ferredoxin-dependent nitrite reductase from spinach leaves
Agric. Biol. Chem.
43
659-661
1979
Spinacia oleracea
-
Ida, S.
Purification to homogeneity of spinach nitrite reductase by ferredoxin-sepharose affinity chromatography
J. Biochem.
82
915-918
1977
Spinacia oleracea
Hirasawa, M.; Knaff, D.B.
Interaction of ferredoxin-linked nitrite reductase with ferredoxin
Biochim. Biophys. Acta
830
173-180
1985
Spinacia oleracea
-
Hirasawa-Soga, M.; Tamura, G.
Some properties of ferredoxin-nitrite reductase from Spinacia oleracea
Agric. Biol. Chem.
45
1615-1620
1981
Spinacia oleracea
-
Hirasawa-Soga, M.; Horie, S.; Tamura, G.
Further characterization of ferredoxin nitrite reductase and the relationship between the enzyme and methyl viologen-dependent nitrite reductase
Agric. Biol. Chem.
46
1319-1328
1982
Spinacia oleracea
-
Vega, J.M.; Kamin, H.
Spinach nitrite reductase. Purification and properties of a siroheme-containing iron-sulfur enzyme
J. Biol. Chem.
252
896-909
1977
Spinacia oleracea
Ramirez, J.M.; Del Campo, F.F.; Paneque, A.; Losada, M.
Ferredoxin-nitrite reductase from spinach
Biochim. Biophys. Acta
118
58-71
1966
Spinacia oleracea
Bellissimo, D.B.; Privalle, L.S.
Expression of spinach nitrite reductase in Escherichia coli: site-directed mutagenesis of predicted active site amino acids
Arch. Biochem. Biophys.
323
155-163
1995
Spinacia oleracea
Dose, M.M.; Hirasawa, M.; Kleis-Sanfrancisco, S.; Lew, E.L.; Knaff, D.B.
The ferredoxin-binding site of ferredoxin:nitrite oxidoreductase. Differential chemical modification of the free enzyme and its complex with ferredoxin
Plant Physiol.
114
1047-1053
1997
Spinacia oleracea, Spinacia oleracea (P05314)
Hirasawa, M.; de Best, J.H.; Knaff, D.B.
The effect of lysine- and arginine-modifying reagents on spinach ferredoxin:nitrite oxidoreductase
Biochim. Biophys. Acta
1140
304-312
1993
Spinacia oleracea
-
Hirasawa, M.; Dose, M.M.; Kleis-SanFrancisco, S.; Hurley, J.K.; Tollin, G.; Knaff, D.B.
A conserved tryptophan at the ferredoxin-binding site of ferredoxin:nitrite oxidoreductase
Arch. Biochem. Biophys.
354
95-101
1998
Spinacia oleracea
Hirasawa, M.; Proske, P.A.; Knaff, D.B.
The role of tryptophan in the reaction catalyzed by spinach ferredoxin-dependent nitrite reductase
Biochim. Biophys. Acta
1187
80-88
1994
Spinacia oleracea
-
Hirasawa, M.; Tollin, G.; Salamon, Z.; Knaff, D.B.
Transient kinetic and oxidation-reduction studies of spinach ferredoxin:nitrite oxidoreductase
Biochim. Biophys. Acta
1185
336-345
1994
Spinacia oleracea
Kuznetsova, S.; Knaff, D.B.; Hirasawa, M.; Setif, P.; Mattioli, T.A.
Reactions of spinach nitrite reductase with its substrate, nitrite, and a putative intermediate, hydroxylamine
Biochemistry
43
10765-10774
2004
Spinacia oleracea
Kuznetsova, S.; Knaff, D.B.; Hirasawa, M.; Lagoutte, B.; Setif, P.
Mechanism of spinach chloroplast ferredoxin-dependent nitrite reductase: spectroscopic evidence for intermediate states
Biochemistry
43
510-517
2004
Spinacia oleracea
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