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2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
?
chlorate + NADPH
chlorite + NADP+
-
lower affinity than to nitrate, appears to be toxic or its product
-
?
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+ + H2O
-
-
-
-
r
NAD(P)H + H+ + nitrate
NAD(P)+ + nitrite + H2O
NADPH + nitrate
NADP+ + nitrite
-
-
-
-
?
nitrate + NADH + H+
nitrite + NAD+ + H2O
-
-
-
-
r
nitrate + NADPH
nitrite + NADP+
nitrate + NADPH
nitrite + NADP+ + H2O
nitrate + NADPH + H+
nitrite + NADP+
-
-
-
?
nitrate + NADPH + H+
nitrite + NADP+ + H2O
nitrate + reduced anthraquinone 2-sulfonate
nitrite + anthraquinone 2-sulfonate
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
reduced methyl viologen + nitrate
oxidized methyl viologen + nitrite + H2O
additional information
?
-
NAD(P)H + H+ + nitrate
NAD(P)+ + nitrite + H2O
A0A8D3X5C3; A0A8D3X5J3
-
-
-
?
NAD(P)H + H+ + nitrate
NAD(P)+ + nitrite + H2O
A0A8D3X5C3; A0A8D3X5J3
-
-
-
?
nitrate + NADPH
nitrite + NADP+
-
-
-
-
?
nitrate + NADPH
nitrite + NADP+
-
enzyme is essential for reduction of nitrate to ammonia, under oxic conditions the enzyme is involved in nitrate assimilation, under anoxic conditions the enzyme is used for dissimilatory nitrate reduction, transcription regulation mechanism via ammonium, nitrate, and O2 concentrations, overview
-
-
?
nitrate + NADPH
nitrite + NADP+
-
-
-
?
nitrate + NADPH
nitrite + NADP+
enzyme is involved in nitrate assimilation
-
-
?
nitrate + NADPH
nitrite + NADP+
-
-
-
?
nitrate + NADPH
nitrite + NADP+
enzyme is involved in nitrate assimilation, it serves the nitrogen nutrition of the host plant of Tuber borchii in symbiosis
-
-
?
nitrate + NADPH
nitrite + NADP+
-
-
-
?
nitrate + NADPH
nitrite + NADP+
enzyme is involved in nitrate assimilation, it serves the nitrogen nutrition of the host plant of Tuber borchii in symbiosis
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
some mutants use hypoxanthine as nitrogen source, 4.5-S cytochrome-c reductase activity
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
4 activities: NADPH-nitrate reductase, FADH-nitrate reductase, reduced methyl viologen-nitrate reductase and NADPH-cytochrome c reductase
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
two associated activities: cytochrome c reductase and reduced viologen dye:nitrate reductase
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
catalyzes the NADPH-linked reduction of ferricyanide and 2,6-dichlorophenolindophenol, chlorate- and bromate-dependent NADPH oxidation, and FMNH-linked nitrate reduction
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
some mutants use hypoxanthine as nitrogen source, 4.5-S cytochrome-c reductase activity
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
associated cytochrome c reductase activity
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
key enzyme in the assimilation path of nitrate to ammonium. Crude extracts possess endogenous NADPH regenerating systems capable of providing reducing equivalents for effective nitrate reduction in vitro
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
20-fold higher activity with NADPH than with NADH
-
ir
nitrate + NADPH
nitrite + NADP+ + H2O
-
4 activities: NADPH-nitrate reductase, FADH-nitrate reductase, reduced methyl viologen-nitrate reductase and NADPH-cytochrome c reductase
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
4 activities: NADPH-nitrate reductase, FADH-nitrate reductase, reduced methyl viologen-nitrate reductase and NADPH-cytochrome c reductase
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
4 activities: NADPH-nitrate reductase, FADH-nitrate reductase, reduced methyl viologen-nitrate reductase and NADPH-cytochrome c reductase
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
associated FAD-nitrate reductase and methylviologen-nitrate activity
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
first step in nitrate assimilation
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
key enzyme in the assimilation path of nitrate to ammonium. Crude extracts possess endogenous NADPH regenerating systems capable of providing reducing equivalents for effective nitrate reduction in vitro
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
first step in the reduction of nitrate to ammonia, biosynthesis of amino acids and other nitrogen-containing cell constituents
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
20-fold higher activity with NADPH than with NADH
-
ir
nitrate + NADPH
nitrite + NADP+ + H2O
-
4 activities: NADPH-nitrate reductase, FADH-nitrate reductase, reduced methyl viologen-nitrate reductase and NADPH-cytochrome c reductase
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
first step in the reduction of nitrate to ammonia, biosynthesis of amino acids and other nitrogen-containing cell constituents
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
-
-
?
nitrate + NADPH + H+
nitrite + NADP+ + H2O
-
-
-
-
?
nitrate + NADPH + H+
nitrite + NADP+ + H2O
-
-
-
-
?
nitrate + NADPH + H+
nitrite + NADP+ + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
-
-
-
-
?
reduced methyl viologen + nitrate
oxidized methyl viologen + nitrite + H2O
A0A8D3X5C3; A0A8D3X5J3
the optimum electron donor is methyl viologen plus Na2S2O4
-
-
?
reduced methyl viologen + nitrate
oxidized methyl viologen + nitrite + H2O
A0A8D3X5C3; A0A8D3X5J3
the optimum electron donor is methyl viologen plus Na2S2O4
-
-
?
additional information
?
-
enzyme expression is regulated by different inorganic and organic nitrogen sources, e.g. nitrate, ammonium, urea and glutamate, regulatory mechanism of nitrate aquisition in ectomycchorizae, overview
-
-
?
additional information
?
-
-
NADPH-dependent cytochrome c reducing activity by the holo-enzyme is determined with FAD and NADPH spectroscopically at 550 nm and 340 nm. Apo-nitrate reductase has a marginally lower, about 10% reduced cytochrome c reducing activity, which correlates to its 15% reduced heme content
-
-
?
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iodoacetamide
-
pH 7.5, 40% inhibition at 1 mM
NADP+
-
inhibits NADPH oxidation, non-competitive with respect to nitrate
NH4+
-
inhibits the enzyme under aerobic conditions
nitrite
-
competitive with respect to nitrate and non-competitive to NADPH
phenanthroline hydrate
-
pH 7.5, 1:10, 20% inhibition at 0.1 mM
Phenylglyoxal
-
in 0.1 M phosphate, pH 7.3, 4 mM, inactivation after 15 min to 40% and to 20% after 60 min
potassium chlorate
-
pH 7.5, slight, 20% inhibition at 5 mM
potassium ethyl xanthate
-
-
Sodium nitrite
-
pH 7.5, slight, 50% inhibition at 5 mM
8-hydroxyquinoline
-
pH 7.5, 20% inhibition at 0.1 mM
8-hydroxyquinoline
-
94% inhibition at 10 mM
azide
-
pH 7.5, 90% inhibition at 0.01 mM
azide
-
96% inhibition at 5 mM
Cu2+
-
inhibitory
Cu2+
A0A8D3X5C3; A0A8D3X5J3
1 mM, 76% of initial activity
cyanide
-
pH 7.5, 100% inhibition at 0.01 mM
cyanide
-
99% inhibition at 10 mM
cyanide
-
1-10 mM inhibits enzyme by 70-90%
NADPH
-
elevated concentrations
NADPH
-
elevated concentrations
p-chloromercuribenzoate
-
reversion of the inhibition by addition of reduced glutathione
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
reversed by cysteine or glutathione
p-hydroxymercuribenzoate
-
pH 7.5, 85% inhibition at 0.001 mM
p-hydroxymercuribenzoate
-
reversed by sulfhydryl reagents
p-hydroxymercuribenzoate
-
at 0.1 mM complete inhibition
additional information
-
cysteine or dithiothreitol relieve or prevent inhibition. Not inhibited by urea, glutamic acid, aspartic acid and ammonia at 10 mM
-
additional information
-
exogenous ammonium represses enzyme expression under oxic conditions in presence or absence of nitrate, while under anoxic conditions the enzyme is expressed even in the presence of ammonium, promotor activity study
-
additional information
-
intracellularly accumulated nitrite can inhibit nitrate uptake, addition of nitrite at concentrations above 5 mM is toxic and causes growth retardation
-
additional information
the nitrogen sources nitrate, glutamate, and urea induce enzyme expression, but ammonium represses it
-
additional information
-
protection of inactivation by FAD and restorage by dithiothreitol
-
additional information
A0A8D3X5C3; A0A8D3X5J3
not inhibitory nor activating: Ba2+, Zn2+, EDTA
-
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?
A0A8D3X5C3; A0A8D3X5J3
x * 87300, electron transfer subunit, x * 80500 catalytic subunit, SDS-PAGE
?
-
x * 87300, electron transfer subunit, x * 80500 catalytic subunit, SDS-PAGE
-
dimer
-
2 * 91000, homodimer, SDS-PAGE, smaller bands are caused by proteolytic cleavage
dimer
-
1 * 130000 + 1 * 115000, SDS-PAGE, homodimer of 2 * 150000 suggested
dimer
-
monodimer, 2 * 145000
dimer
-
2 * 97000: nit-3 enzyme, 2 * 132000, wild-type
dimer
in presence of molybdenum cofactor, enzyme forms a dimer, gel filtration, sedimentation velocity analysis
dimer
-
1 * 130000 + 1 * 115000, SDS-PAGE, homodimer of 2 * 150000 suggested
-
heterotrimer
-
1 * 125000 + 1 * 60000 + 1 * 25000, SDS-PAGE
heterotrimer
-
1 * 125000 + 1 * 60000 + 1 * 25000, SDS-PAGE
-
homodimer
-
holo-enzyme, determination with SDS-PAGE, gel filtration and analytical ultracentrifugation. The enzyme has a largely hydrophobic dimer interface
multimer
-
-
tetramer
-
2 * 59000 + 2 * 38000, SDS-PAGE, after heat-treatment all polypeptide chains are 59 kDa
additional information
-
nit-1 mutant enzyme is the apoprotein of nitrate reductase
additional information
-
nit-1 mutant enzyme is the apoprotein of nitrate reductase
additional information
-
aggregate of two different polypeptide chains: one responsible for transport of electrons fom NADPH to FAD or cytochrome c, nit-1 enzyme. The other transfers electrons from FAD via molybdenum to nitrate, nit-3 enzyme
additional information
-
at least 2 subunits suggested
additional information
-
the apo-enzyme dissociates completely into monomers, the ratio between monomeric and dimeric apo-NR does not change significantly upon a 20fold dilution. Active site formation of eukaryotic nitrate reductase is an autonomous process intrinsically tied to nitrate reductase dimerization, molybdenum cofactor-dependent enzyme maturation, overview. Enzyme domain structure, overview
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G811V
-
site-directed mutagenesis, an FAD-binding mutant
H654A/H677A
-
site-directed mutagenesis, CD spectroscopy shows no negative effects of the introduced mutations on protein secondary structure in comparison to the wild-type protein, but the mutant contains no heme, while the FAD binding ability is not significantly disturbed
R778E
-
site-directed mutagenesis, an FAD-binding mutant. The mutant binds essentially the same amount of Moco as does the wild type protein
R921S
-
little impact on NADPH and NADH activity, no importance for pyridine nucleotide specificity
R921T
-
little impact on NADPH and NADH activity, no importance for pyridine nucleotide specificity
R932Q
-
1/4 wild type NADPH activity is retained, twice as much NADH activity is present as compared to wild type
R932S
-
1/10 wild type NADPH activity is retained, 2/3 of wild type NADH activity
S920D
-
important for the enzyme's interaction with the pyridine nucleotide substrates. Mutant retains ~2% of the NADPH activity of the wild type while it has an increased NADH activity, ~15% higher. It is concluded that Ser920 is a ligand involved in binding the 2' phosphate of NADPH in the wild type enzyme
S920D/R932S
-
greatest decrease in NADPH activity of all created mutants, shows that Arg932 is a residue interacting with the pyridine nucleotide coenzyme electron donors and that Ser920 and Arg932 have effects on substrate binding and catalytic activity. Both residues may be ligands to the 2' phosphate of NADPH in the wild type cyt b reductase fragment of nitrate reductase
Y780A
-
site-directed mutagenesis, an FAD-binding mutant
additional information
-
studies of temperature-sensitive mutations, niaD gene: mutation leads to loss of a 4.5-S cytochrome-c reductase activity, which is a subunit of nitrate reductase. It is suggested that neither the product of the cnxE nor the cnyF genes form part of the nitrate reductase molecule, but some catalytic role in cofactor formation, niaD and cnxH seem to be structural genes
additional information
-
different structural gene (niaD) and cofactor gene (cnx) mutants are analyzed concerning their flavin and molybdenum content
additional information
-
construction of null-mutants of gene niaD
additional information
-
studies of temperature-sensitive mutations, niaD gene: mutation leads to loss of a 4.5-S cytochrome-c reductase activity, which is a subunit of nitrate reductase. It is suggested that neither the product of the cnxE nor the cnyF genes form part of the nitrate reductase molecule, but some catalytic role in cofactor formation, niaD and cnxH seem to be structural genes
-
additional information
-
the purified native enzyme is successfully used for synthesis of silver nanoparticles in an NADPH-dependent manner using gelatin as a capping agent, analysis by X-ray diffraction, dynamic light scattering spectroscopy, and transmission and scanning electron microscopy, overview. 0.2 M Phosphate buffer, pH 7.2, 1 mM silver nitrate as the enzyme substrate, 0.1 mg gelatin as a capping agent, 1 mM 4-hydroxyquinoline as an electron carrier, 1 mM NADPH as enzyme cofactor, and 0.1 mg of purified fungal nitrate reductase are incubated at 25°C for 5 h. The stable nonaggregating nanoparticles are spherical in shape with an average size of 50 nm and a zeta potential of -34.3. The synthesized nanoparticles show a strong growth inhibitory antimicrobial activity against all tested human pathogenic fungi and bacteria, overview
additional information
-
the purified native enzyme is successfully used for synthesis of silver nanoparticles in an NADPH-dependent manner using gelatin as a capping agent, analysis by X-ray diffraction, dynamic light scattering spectroscopy, and transmission and scanning electron microscopy, overview. 0.2 M Phosphate buffer, pH 7.2, 1 mM silver nitrate as the enzyme substrate, 0.1 mg gelatin as a capping agent, 1 mM 4-hydroxyquinoline as an electron carrier, 1 mM NADPH as enzyme cofactor, and 0.1 mg of purified fungal nitrate reductase are incubated at 25°C for 5 h. The stable nonaggregating nanoparticles are spherical in shape with an average size of 50 nm and a zeta potential of -34.3. The synthesized nanoparticles show a strong growth inhibitory antimicrobial activity against all tested human pathogenic fungi and bacteria, overview
-
additional information
-
nit-1 mutant: lacks all activities except FAD-dependent NADPH:cytochrome c reductase activity,nit-2 mutant: reduced FAD:- and reduced methyl viologen:nitrate reductase activities but lacks the other two activities
additional information
-
nit-3 mutant (FGSC 262): reduced FAD-nitrate reductase and reduced methylviologen-nitrate reductase activities
additional information
-
nit-1 mutant, suggested to produce the complete apoenzyme
additional information
-
several mutations of recombinant cyt b reductase fragment of nitrate reductase in the region Ser920, Arg921 and Arg932 are created. Conversion from NADPH-specific to virtually NADH-specific cyt b reductase fragment of nitrate reductase
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-10°C, 0.1 M sodium phosphate buffer, pH 7.3, 0.17 M NaCl, 1 mM dithiothreitol, 5 m M EDTA, 0.5 mM PMSF, 1%ethanol, 30% glycerol
-
-10°C, 50 mM sodium phosphate, pH 6.9, 30% glycerol, 0.5 mM EDTA, 0.5 mM dithiothreitol, 0.5 mM phenylmethylsulfonylfluoride, 0.1 mM FAD, stable for at least 6 months
-
-15°C, fraction II, most stable, optimal pH: 7.0, 10-20% loss of activity after a month
-
-15°C, fraction IV, one week, loses about half of its activity
-
-15°C, fraction V, quite unstable, overnight, loses at least half of its activity
-
-20°C, stable for 6 months or longer, 5% loss of activity
-
-80°C, 0.02 mM FAD, several months with only slight loss of the activity
-
-80°C, 25 mM Mops, 0.1 mM EDTA, pH 7.2
-
-80°C, extract, 6 months, without loss of activity
-
4°C or -15°C, fraction III, overnight, 50% loss of activity
-
4°C, half life of 3-5 days
-
5°C, urea-treated, 0.1 M potassium phosphate buffer, pH 7.3, 5 mM EDTA, 2 mM dithioerythritol, 0.5 mg/ml or more bovine serum albumin, stable for 18 h without loss of activity
-
half life of about 2 h with ammonium sulfate or ammonium chloride as sole N-source
-
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ammonium slufate precipitation, ion-exchange, gel filtration, hydroxylapatite column. FAD and EDTA essential in all buffers during purification
-
ammonium sulfate precipitation
-
immobilized metal affinity chromatography and SourceQ15 column anion exchange chromatography
-
ion-exchange, ammonium sulfate precipitation, gel filtration
-
metal-chelate affinity chromatography for his-tagged proteins, ammonium sulfate fractionation, affinity chromatography
-
native enzyme 70fold by ultrafiltration, anion exchange chromatography, and gel filtration
-
partially purification of wild-type and nit-3 mutant by streptomycin sulfate precipitation and ammonium sulfate fractionation, of nit-1 mutant by protamine sulfate fractionation, ammonium sulfate precipitation and gel filtration
-
protamine sulfate and ammonium sulfate precipitation, hemoglobin-Sepharose column, Bio-Gel A, FAD-Sepharose affinity column. proteolysis during extensive purification
-
quick purification by immunoprecipitation with monospecific anti-nitrate reductase serum, stabilization during purification and protection of proteolytic cleavage by addition of phenylmethylsulphonyl fluoride
-
recombinant enzyme from Escherichia coli strains TP1000, RK5206, and RK5204 by a two-step affinity purification
-
salt fractionation, gel filtration , ion-exchange
-
streptomycin sulfate and ammonium sulfate precipitation, ion-exchange, gel filtration, isoelectric focusing, FAD-affinity
-
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MacDonald, D.W.; Cove, D.J.
Studies on temperature-sensitive mutants affecting the assimilatory nitrate reductase of Aspergillus nidulans
Eur. J. Biochem.
47
107-110
1974
Aspergillus nidulans, Aspergillus nidulans biA-1
brenda
McDonald, D.W.; Coddington, A.
Properties of the assimilatory nitrate reductase from Aspergillus nidulans
Eur. J. Biochem.
46
169-178
1974
Aspergillus nidulans
brenda
Padidam , M.; Venkateswarlu, K.; Johri, M.M.
Ammonium represses NADPH-nitrate reductase in the moss Funaria hygrometrica
Plant Sci.
75
185-194
1991
Funaria hygrometrica
-
brenda
Pan, S.S.; Nason, A.
Purification and characterization of homogeneous assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase from Neurospora crassa
Biochim. Biophys. Acta
523
297-313
1978
Neurospora crassa, Neurospora crassa STA4
brenda
Minagawa, N.; Yoshimoto, A.
Purification and characterization of the assimilatory NADPH-nitrate reductase of Aspergillus nidulans
J. Biochem.
91
761-774
1982
Aspergillus nidulans
brenda
Cooley, R.N.; Tomsett, A.B.
Determination of the subunit size of NADPH-nitrate reductase from Aspergillus nidulans
Biochim. Biophys. Acta
831
89-93
1985
Aspergillus nidulans
-
brenda
Downey, R.J.
The role of molybdenum in formation of the NADPH-nitrate reductase by Aspergillus nidulans
Biochem. Biophys. Res. Commun.
50
920-925
1973
Aspergillus nidulans
brenda
Nicholas, D.J.D.; Nason, A.
Molybdenum and nitrate reductase. II. Molybdenum as a constituent of nitrate reductase
J. Biol. Chem.
207
353-360
1954
Neurospora crassa
brenda
Nason, A.; Evans, H.J.
Triphosphopyridine nucleotide-nitrate reductase in Neurospora
J. Biol. Chem.
202
655-673
1953
Neurospora crassa, Neurospora crassa 5297a
brenda
Shiraishi, N.; Croy, C.; Kaur, J.; Campbell, W.H.
Engineering of pyridine nucleotide specificity of nitrate reductase: mutagenesis of recombinant cytochrome b reductase fragment of Neurospora crassa NADPH:nitrate reductase
Arch. Biochem. Biophys.
358
104-115
1998
Neurospora crassa
brenda
Savidov, N.A.; Alikulov, Z.A.; Lips, S.H.
Identification of an endogenous NADPH-regenerating system coupled to nitrate reduction in vitro in plant and fungal crude extracts
Plant Sci.
133
33-45
1998
Hordeum vulgare, Neurospora crassa
-
brenda
Horner, R.D.
Purification and comparison of nit-1 and wild-type NADPH:nitrate reductases of Neurospora crassa
Biochim. Biophys. Acta
744
7-15
1983
Neurospora crassa
-
brenda
Downey, R.J.
Characterization of the reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase of Aspergillus nidulans
J. Bacteriol.
105
759-768
1971
Aspergillus nidulans
brenda
Tachiki, T.; Nason, A.
Preparation and proterties of apoenzyme of nitrate reductases from wild-type and nit-3 mutant of Neurospora crassa
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