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Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Escherichia coli and UniProt Accession P28861
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1.18.1.2 ferredoxin-NADP+ reductaseIUBMB Comments
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.
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Word Map
- 1.18.1.2
- nitrate
- ferredoxins
-
denitrification
-
denitrify
- reductases
- heme
- fad
- spinach
- chloroplast
- copper
- ammonia
-
nitrous
- flavin
-
dissimilatory
- photosystems
- flavodoxins
- denitrificans
- alcaligenes
- paracoccus
- n2o
- anabaena
-
copper-containing
- thylakoids
-
anammox
- p450scc
- semiquinone
- diaphorase
- viologen
- azurins
-
ferredoxin-dependent
- stutzeri
-
plant-type
- achromobacter
-
flavoenzymes
-
electron-transfer
-
ammonia-oxidizing
- plastocyanin
-
dinitrogen
-
photoreduction
- gogat
- pregnenolone
-
nitrate-induced
- xylosoxidans
-
photoreduced
-
wolinella
- isoalloxazine
-
nitrate-reducing
- biotechnology
- nitrosomonas
-
deoxyhemoglobin
- agriculture
-
single-electron
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
nitrite reductase, adrenodoxin reductase, ferric reductase, ferredoxin-nadp+ reductase, ferredoxin-nadp reductase, ferredoxin-nadp(+) reductase, ferredoxin-nadp+ oxidoreductase, flavodoxin reductase, ferredoxin:nadp+ oxidoreductase, ferredoxin:nadp+ reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adrenodoxin reductase
-
-
-
-
DA1
-
-
-
-
ferredoxin-NADP oxidoreductase
-
-
-
-
ferredoxin-NADP reductase
-
-
-
-
Ferredoxin-NADP(+) reductase
-
-
-
-
ferredoxin-NADP-oxidoreductase
-
-
-
-
ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
-
-
-
-
ferredoxin-TPN reductase
-
-
-
-
ferredoxin:NADP+ oxidoreductase
-
-
-
-
Flavodoxin reductase
-
-
-
-
FLDR
-
-
-
-
FLXR
-
-
-
-
FNR
NADP:ferredoxin oxidoreductase
-
-
-
-
NADPH:ferredoxin oxidoreductase
-
-
-
-
NFR
-
-
-
-
reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
-
-
-
-
reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
-
-
-
-
TPNH-ferredoxin reductase
-
-
-
-
FNR
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
reaction mechanism
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
catalytic mechanism of forward and reverse reactions
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
reaction mechanism via semiquinone intermediate and radical formation
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
reaction mechanism, substrate recognition mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NADP+ oxidoreductase
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.
CAS REGISTRY NUMBER
COMMENTARY
56367-57-8
-
9029-33-8
-
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 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
best substrate
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
?
2 ferrocytochrome c + NAD+ + H+
2 ferricytochrome c + NADH
NADH, poor substrate
-
-
?
2 oxidized ferredoxin + NADH + H+
2 reduced ferredoxin + NAD+
NADH, poor substrate
-
-
?
2 oxidized ferredoxin + NADPH + H+
2 reduced ferredoxin + NADP+
source of ferredoxin: Pisum sativum
-
-
?
Fe(III)-diethylenetriamine-N,N,N',N'',N''-pentaacetic acid + NADPH + H+
Fe(II) + diethylenetriamine-N,N,N',N'',N''-pentaacetic acid + NADP+
highest activity
-
-
?
Fe(III)-nitrilotriacetic acid + NADPH + H+
Fe(II) + nitrilotriacetic acid + NADP+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
diaphorase reaction
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
r
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
ferredoxin is the preferred electron acceptor
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
substrate is a bulky protein
-
-
r
additional information
?
-
-
the enzyme reduces flavodoxin I and flavodoxin II, reaction of EC 1.19.1.1, and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Ferredoxin binds to FNR with high affinity (Kd below 0.5 microM) and is reduced under single-turnover conditions. Flavodoxin I and flavodoxin II show affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin
-
-
?
additional information
?
-
the enzyme reduces flavodoxin I and flavodoxin II, reaction of EC 1.19.1.1, and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Ferredoxin binds to FNR with high affinity (Kd below 0.5 microM) and is reduced under single-turnover conditions. Flavodoxin I and flavodoxin II show affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin
-
-
?
additional information
?
-
-
enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
specificity for tightly bound electron acceptors, overview
-
-
?
additional information
?
-
specificity for tightly bound electron acceptors, overview
-
-
?
additional information
?
-
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible
-
-
?
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
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism
-
-
r
additional information
?
-
-
the enzyme reduces flavodoxin I and flavodoxin II, reaction of EC 1.19.1.1, and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Ferredoxin binds to FNR with high affinity (Kd below 0.5 microM) and is reduced under single-turnover conditions. Flavodoxin I and flavodoxin II show affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin
-
-
?
additional information
?
-
the enzyme reduces flavodoxin I and flavodoxin II, reaction of EC 1.19.1.1, and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Ferredoxin binds to FNR with high affinity (Kd below 0.5 microM) and is reduced under single-turnover conditions. Flavodoxin I and flavodoxin II show affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin
-
-
?
additional information
?
-
-
enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
-
involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions
NADP+
-
binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview
NADPH
-
binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
inhibition of electron transfer at higher electron acceptor rate
-
flavodoxinI/II
inhibition of electron transfer at higher electron acceptor rate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00364
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.0396
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.003
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.0018
NADPH
in the presence of 0.15 mM Fe(III)-EDTA, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.003
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.0036
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
0.0018
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
0.0076
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
kinetics, rapid thermal inactivation of reduced enzyme and drop of activity
-
additional information
additional information
-
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
-
additional information
additional information
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C
3.53
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C
45.3
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
24.5
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
99
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
3.7
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
19.4
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
520
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
additional information
additional information
-
the low efficiency is intrinsic to the reductase itself
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
76.3
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C
972
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C
15
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
6800
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
33000
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
500
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
10700
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
insertion mutants lacking a functional enzyme do not require methionine and grow well anaerobically, but they show increased sensitivity to paraquat
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. The plastidic enzyme lacking the beta-hairpin is unable to fold properly. An extra tryptophan at the carboxy terminus, emulating the bacterial enzyme, results in an enzyme with decreased affinity for FAD and reduced diaphorase and ferredoxin-dependent cytochrome c reductase activities. The insertion of the beta-hairpin into the corresponding position of the bacterial enzyme increases FAD affinity but does not affect its catalytic properties. The same insertion with simultaneous deletion of the carboxyterminal tryptophan produces a bacterial chimera emulating the plastidic architecture with an increased kcat and an increased catalytic efficiency for the diaphorase activity and a decrease in the enzymes ability to react with its substrates ferredoxin and flavodoxin. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
inactivation of the enzyme due to irreversible protein unfolding and dissociation of the FADH2 cofactor, slower process with binding of ferredoxin, FAD, or flavodoxin, best by riboflavin, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl Toyopearl column chromatography and DEAE Sepharose column chromatography
soluble enzyme by ultracentrifugation, DEAE ion exchange chromatography, dialysis, and hydroxyapatite chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the level of Fpr is significantly increased in Escherichia coli cultured in lower iron concentrations (0.017-12.2 ppm)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
enzyme can be an electron source in biotechnological applications
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, Escherichia coli (P28861)
Ceccarelli, E.A.; Arakaki, A.K.; Cortez, N.; Carrillo, N.
Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases
Biochim. Biophys. Acta
1698
155-165
2004
Azotobacter vinelandii, Anabaena sp., Chlamydomonas reinhardtii, Cyanophora paradoxa, Escherichia coli, Leptospira interrogans, Rhodobacter capsulatus, Spinacia oleracea, Anabaena sp. PCC7119
Carrillo, N.; Ceccarelli, E.A.
Open questions in ferredoxin-NADP+ reductase catalytic mechanism
Eur. J. Biochem.
270
1900-1915
2003
Azotobacter vinelandii, Anabaena sp., Capsicum annuum, Cyanobacteria, Escherichia coli, Pisum sativum, Rhodobacter capsulatus, Spinacia oleracea, Zea mays
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
Medina, M.; Gomez-Moreno, C.
Interaction of ferredoxin-NADP+ reductase with its substrates: optimal interaction for efficient electron transfer
Photosynth. Res.
79
113-131
2004
Azotobacter vinelandii, Anabaena sp., Escherichia coli, Spinacia oleracea
Takeda, K.; Sato, J.; Goto, K.; Fujita, T.; Watanabe, T.; Abo, M.; Yoshimura, E.; Nakagawa, J.; Abe, A.; Kawasaki, S.; Niimura, Y.
Escherichia coli ferredoxin-NADP+ reductase and oxygen-insensitive nitroreductase are capable of functioning as ferric reductase and of driving the Fenton reaction
Biometals
23
727-737
2010
Escherichia coli (P28861), Escherichia coli
Musumeci, M.A.; Botti, H.; Buschiazzo, A.; Ceccarelli, E.A.
Swapping FAD binding motifs between plastidic and bacterial ferredoxin-NADP(H) reductases
Biochemistry
50
2111-2122
2011
Pisum sativum (P10933), Escherichia coli (P28861)
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)
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), Escherichia coli
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