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Information on EC 1.19.1.1 - flavodoxin-NADP+ reductase
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1.19.1.1 flavodoxin-NADP+ reductaseIUBMB Comments
A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin---NADP+ reductase.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
Bc_0385, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin/flavodoxin-NADP(H) oxidoreductase, FLDR, FNR, FPR, PETH, YumC, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bc_0385
ferredoxin/flavodoxin-NADP(H) oxidoreductase
FLDR
FPR
PETH
YumC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH + H+
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
flavodoxin:NADP+ oxidoreductase
A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin---NADP+ reductase.
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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
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
-
-
-
?
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
-
?
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
-
-
-
-
r
oxidized cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
?
additional information
?
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the enzyme reduces flavodoxin I, flavodoxin II and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner, i.e. reaction of EC 1.18.2.1. Flavodoxin I and flavodoxin II behave similarly with respect to FNR, with affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin. Flavodoxin I and flavodoxin II can obtain electrons from reduced Fd at rates that are comparable to those obtained with reduced FNR
-
-
?
additional information
?
-
-
substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein
-
-
?
additional information
?
-
-
the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples
-
-
?
additional information
?
-
Escherichia coli B / ATCC 11303
-
substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein
-
-
?
additional information
?
-
-
the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples
-
-
?
additional information
?
-
no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
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-
?
additional information
?
-
no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
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-
?
additional information
?
-
enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
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-
?
additional information
?
-
-
enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
-
-
?
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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
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
?
additional information
?
-
the enzyme reduces flavodoxin I, flavodoxin II and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner, i.e. reaction of EC 1.18.2.1. Flavodoxin I and flavodoxin II behave similarly with respect to FNR, with affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin. Flavodoxin I and flavodoxin II can obtain electrons from reduced Fd at rates that are comparable to those obtained with reduced FNR
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
oxidized FLDR has flavin absorbance maxima at 456 nm and 400 nm, with a shoulder on the longer wavelength band at 483 nm
FAD
reduction of the FAD moiety of phenylglyoxal-modified FNR by laser-generated 5-deazariboflavin semiquinone occurs with a second-order rate constant 2.5fold smaller than that obtained for reduction of native FNR
NADP+
Kd value 0.222 mM, coenzyme docking occurrs through the 2'-P-AMP moiety
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavodoxin
cytochrome c reductase activity of FPR is stimulated three times by the addition of flavodoxin
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
ferricytochrome c
presence of flavodoxin, pH 8.0, temperature not specified in the publication
0.009
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.02
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.039
NADPH
mutant A266Y/Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.08
NADPH
substrate ferricyanide, pH 8.0, temperature not specified in the publication
0.085
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
ferricytochrome c
presence of flavodoxin, pH 8.0, temperature not specified in the publication
1
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
7
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
7.2
NADPH
substrate ferricyanide, pH 8.0, temperature not specified in the publication
8
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
12
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
20
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
Uniprot
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
brenda
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Escherichia coli cells deficient in the soxRS-induced ferredoxin (flavodoxin)-NADP(H) reductase FPR, display abnormal sensitivity to methyl viologen. Neither bacteriostatic effects nor inactivation of oxidant-sensitive hydrolyases can be detected in mutant cells exposed to methyl viologen. FPR inactivation does not affect the methyl viologen-driven soxRS response, FPR overexpression leads to enhanced stimulation of the regulon, with concomitant oxidation of the NADPH pool. Accumulation of a site-directed FPR mutant that uses NAD(H) instead of NADP(H) has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
physiological function
flavodoxin, flavodoxin reductase and NADPH function during the activation of the anaerobic ribonucleotide reductase
physiological function
insertion mutants lacking a functional enzyme do not require methionine and grow well anaerobically, but they show increased sensitivity to paraquat
Show AA Sequence and Transmembrane Helices (1691 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
monomer
-
1 * 27620, calculated, 1 * 27 648, electrospray mass spectroscopy
-
additional information
the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
additional information
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the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
-
additional information
the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure to 2.5 A resolution, orthorhombic space group P21212, with unit-cell parameters a = 57.2, b = 164.3, c = 95.0 A, containing two protein molecules in the asymmetric unit
molecular modelling indicates that movement of the C-terminal tryptophan (W248) is necessary to permit close approach of the nicotinamide ring of NADPH to the flavin. Residues R174 and R184 are located close to the adenosine ribose 2'-phosphate group, and R144 is likely to interact with the nicotinamide ribose 5'-phosphate group
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a multiscale modelling approach for analysis of the electron transfer process in complexes of the enzyme with both ferredoxin and flavodoxin, reactions of EC 1.19.1.1 and EC1.18.1.2, respectively. The electron transfer in FNR/ferredoxin proceedes through a bridge-mediated mechanism in a dominant protein-protein complex, where transfer of the electron is facilitated by ferredoxin loop-residues 40-49. In FNR/flavodoxin, a direct transfer between redox cofactors is observed and less complex specificity than in ferredoxin
in complex with 2'-phospho-AMP and NADP+. In the complexes obtained, the nucleotides bind exclusively through the adenosine moiety. The adenosine moiety binds into a cavity formed by residues of conserved segments, i.e residues 128 to 130, residues 158 to 163, residues 193 to 205, and residues 233 to 240. The adenosine binding site is essentially formed by residues R158, R195 and R203, which stabilise the nucleotide
to 2.17 A resolution, tetragonal space group P41212, with unit-cell parameters a = b = 66.49, c = 121.32 A
no perturbation of the 31P-NMR resonances assigned to the FAD moiety of FNR or the FMN and phosphodiester moieties of Azotobacter flavodoxin are observed on complexation of Azotobacter flavodoxin and Spinacia oleracea FNR. Reduction of FMN to its semiquinone form results in extensive line-broadening of the FMN resonance. The FAD resonances of the FNR-flavodoxin complex are unaffected by FMN semiquinone formation. The distance from the FMN phosphate to the flavin ring is altered on binding the flavodoxin to FNR
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y50G
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50S
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50W
mutation results in a blue shift of the FAD transition bands, with quenching of fluorescence emission. Mutant displays decreased thermal stability
Y50G
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
Y50S
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
R144A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
R174A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
R184A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
Y308S
mutant uses NAD(H) instead of NADP(H), expression of the mutant has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
R144A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R174A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R184A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
Y303F
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
Y303S
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y303F
-
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
-
Y303S
-
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
-
Y308F
about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin
Y308S
nearly inactive mutant with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y308W
about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin
A266Y
mutant does not allow formation of active charge-transfer complexes, probably due to restraints of C-terminus pliability. Mutant displays higher affinity for NADP+ than wild-type
A266y/Del267-272
deletion/mutation emulates the structure present in plastidic versions of the protein. It does not modify the general geometry of FAD itself, but increases exposure of the flavin to the solvent, prevents a productive geometry of FAD:NADP(H) complex and decreases the protein thermal stability. Mutant displays higher affinity for NADP+ than wild-type
Del267-272
deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
reduced FNR is subject to inactivation due to unfolding of the protein and dissociation of the FADH2 cofactor
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme
-
FNR reduced in the presence of NADPH is slowly inactivated under all conditions. Reactivity towards flavodoxin is lost most rapidly (kinact of 0.031 per min) with less than 10% of the original activity remaining after 30 min, reactivity towards ferredoxin is not as rapidly affected (kinact of 0.0065 per min) with 80% of the original activity remaining after 30 min
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recpmbinant protein. FLDR is bright yellow in its oxidized form and it is converted to a neutral blue semiquinone by the addition of one reducing equivalent
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wan, J.T.; Jarrett, J.T.
Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli
Arch. Biochem. Biophys.
406
116-126
2002
Escherichia coli (P28861)
brenda
Nogues, I.; Tejero, J.; Hurley, J.K.; Paladini, D.; Frago, S.; Tollin, G.; Mayhew, S.G.; Gomez-Moreno, C.; Ceccarelli, E.A.; Carrillo, N.; Medina, M.
Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin
Biochemistry
43
6127-6137
2004
Pisum sativum (P10933), Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
brenda
Jarrett, J.T.; Wan, J.T.
Thermal inactivation of reduced ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli
FEBS Lett.
529
237-242
2002
Escherichia coli
brenda
Bittel, C.; Tabares, L.C.; Armesto, M.; Carrillo, N.; Cortez, N.
The oxidant-responsive diaphorase of Rhodobacter capsulatus is a ferredoxin (flavodoxin)-NADP(H) reductase
FEBS Lett.
553
408-412
2003
Rhodobacter capsulatus (Q9L6V3)
brenda
Crain, A.V.; Broderick, J.B.
Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme
Biochim. Biophys. Acta
1834
2512-2519
2013
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Perez-Dorado, I.; Bortolotti, A.; Cortez, N.; Hermoso, J.A.
Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus
Acta Crystallogr. Sect. F
64
375-377
2008
Rhodobacter capsulatus (D5ATP7), Rhodobacter capsulatus ATCC BAA-309 (D5ATP7)
brenda
Skramo, S.; Hersleth, H.P.; Hammerstad, M.; Andersson, K.K.; Rohr, A.K.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus
Acta Crystallogr. Sect. F
70
777-780
2014
Bacillus cereus (Q81IK1), Bacillus cereus, Bacillus cereus DSM 31 (Q81IK1)
brenda
Bianchi, V.; Eliasson, R.; Fontecave, M.; Mulliez, E.; Hoover, D.M.; Matthews, R.G.; Reichard, P.
Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase
Biochem. Biophys. Res. Commun.
197
792-797
1993
Escherichia coli (P28861)
brenda
Leadbeater, C.; McIver, L.; Campopiano, D.; Webster, S.; Baxter, R.; Kelly, S.; Price, N.; Lysek, D.; Noble, M.; Chapman, S.; Munro, A.
Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase
Biochem. J.
352
257-266
2000
Escherichia coli, Escherichia coli HMS174
brenda
Bortolotti, A.; Perez-Dorado, I.; Goni, G.; Medina, M.; Hermoso, J.A.; Carrillo, N.; Cortez, N.
Coenzyme binding and hydride transfer in Rhodobacter capsulatus ferredoxin/flavodoxin NADP(H) oxidoreductase
Biochim. Biophys. Acta
1794
199-210
2009
Rhodobacter capsulatus (Q9L6V3)
brenda
Bortolotti, A.; Sanchez-Azqueta, A.; Maya, C.M.; Velazquez-Campoy, A.; Hermoso, J.A.; Medina, M.; Cortez, N.
The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme
Biochim. Biophys. Acta
1837
33-43
2014
Rhodobacter capsulatus (Q9L6V3)
brenda
Saen-Oon, S.; Cabeza De Vaca, I.; Masone, D.; Medina, M.; Guallar, V.
A theoretical multiscale treatment of protein-protein electron transfer: The ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems
Biochim. Biophys. Acta
1847
1530-1538
2015
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
brenda
Bonants, P.J.; Mller, F.; Vervoort, J.; Edmondson, D.E.
A 31Pnuclear-magneticresonance study of NADPH-cytochrome-P-450 reductase and of the Azotobacter flavodoxin/ferredoxin-NADP+ reductase complex
Eur. J. Biochem.
190
531-537
1990
Spinacia oleracea (P00455)
brenda
Medina, M.; Gomez-Moreno, C.; Tollin, G.
Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP+ reductase on the kinetics of interprotein electron transfer reactions
Eur. J. Biochem.
210
577-583
1992
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
brenda
McIver, L.; Leadbeater, C.; Campopiano, D.J.; Baxter, R.L.; Daff, S.N.; Chapman, S.K.; Munro, A.W.
Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli
Eur. J. Biochem.
257
577-585
1998
Escherichia coli, Escherichia coli HMS174
brenda
Bianchi, V.; Haggard-Ljungquist, E.; Pontis, E.; Reichard, P.
Interruption of the ferredoxin (flavodoxin) NADP+ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat
J. Bacteriol.
177
4528-4531
1995
Escherichia coli (P28861)
brenda
Krapp, A.R.; Rodriguez, R.E.; Poli, H.O.; Paladini, D.H.; Palatnik, J.F.; Carrillo, N.
The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli
J. Bacteriol.
184
1474-1480
2002
Escherichia coli (P28861)
brenda
Seo, D.; Naito, H.; Nishimura, E.; Sakurai, T.
Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH
Photosynth. Res.
125
321-328
2015
Bacillus subtilis (O05268), Bacillus subtilis 168 (O05268)
brenda
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