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2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
?
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
?
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
oxidized cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
?
additional information
?
-
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + 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+
-
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
-
?
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
-
-
-
-
r
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
-
-
-
-
r
oxidized cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
-
-
-
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+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + 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
-
-
?
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
?
-
-
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
-
-
?
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
-
-
?
additional information
?
-
enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
-
-
?
additional information
?
-
-
enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
-
-
?
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0.0236
ferricyanide
-
pH 7.5, 30°C
0.009
ferricytochrome c
presence of flavodoxin, pH 8.0, temperature not specified in the publication
0.0176
ferricytochrome c2
-
pH 7.5, 30°C
0.0068 - 0.043
reduced flavodoxin
0.0076
reduced flavodoxin I
pH 8.0, 25°C
-
0.004
reduced flavodoxin II
pH 8.0, 25°C
-
0.0017
NADH
-
mutant R184A, pH 7.5, 30°C
0.002
NADH
-
wild-type, pH 7.5, 30°C
0.0051
NADH
-
mutant R144A, pH 7.5, 30°C
0.0099
NADH
-
mutant R174A, pH 7.5, 30°C
0.0039
NADPH
-
pH 7.5, 30°C
0.0039
NADPH
-
wild-type, pH 7.5, 30°C
0.0053
NADPH
-
mutant R144A, pH 7.5, 30°C
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
0.0202
NADPH
-
mutant R174A, pH 7.5, 30°C
0.032
NADPH
mutant A266Y, 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
0.0544
NADPH
-
mutant R184A, pH 7.5, 30°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
0.093
NADPH
wild-type, substrate ferricyanide, pH 7.2, 25°C
0.0068
reduced flavodoxin
-
pH 7.5, 30°C
0.0167
reduced flavodoxin
wild-type, pH 8.0, 25°C
0.017
reduced flavodoxin
mutant Y308W, pH 8.0, 25°C
0.02
reduced flavodoxin
mutant Y308F, pH 8.0, 25°C
0.033
reduced flavodoxin
wild-type, pH 8.0, 25°C
0.043
reduced flavodoxin
mutant Y303F, pH 8.0, 25°C
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26.8
ferricyanide
-
pH 7.5, 30°C
0.25
ferricytochrome c
presence of flavodoxin, pH 8.0, temperature not specified in the publication
2.35
ferricytochrome c2
-
pH 7.5, 30°C
2.5 - 30.6
reduced flavodoxin
0.0042
reduced flavodoxin I
pH 8.0, 25°C
-
0.0039
reduced flavodoxin II
pH 8.0, 25°C
-
0.23
NADH
-
mutant R144A, pH 7.5, 30°C
0.55
NADH
-
wild-type, pH 7.5, 30°C
0.71
NADH
-
mutant R174A, pH 7.5, 30°C
0.84
NADH
-
mutant R184A, pH 7.5, 30°C
1
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
2.2
NADPH
-
mutant R174A, pH 7.5, 30°C
4.03
NADPH
-
mutant R144A, pH 7.5, 30°C
5.1
NADPH
-
mutant R184A, pH 7.5, 30°C
5.65
NADPH
-
wild-type, pH 7.5, 30°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
68
NADPH
mutant A266Y, substrate ferricyanide, pH 7.2, 25°C
222
NADPH
wild-type, substrate ferricyanide, pH 7.2, 25°C
2.5
reduced flavodoxin
mutant Y303W, pH 8.0, 25°C
4
reduced flavodoxin
mutant Y308F, pH 8.0, 25°C
7
reduced flavodoxin
mutant Y303F, pH 8.0, 25°C
8.3
reduced flavodoxin
mutant Y308W, pH 8.0, 25°C
23.3
reduced flavodoxin
wild-type, pH 8.0, 25°C
30.6
reduced flavodoxin
wild-type, pH 8.0, 25°C
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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
-
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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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
-
Y303W
-
almost inactive
-
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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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