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Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Zea mays and UniProt Accession Q9SLP6

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IUBMB 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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This record set is specific for:
Zea mays
UNIPROT: Q9SLP6
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Word Map
The taxonomic range for the selected organisms is: Zea mays
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferredoxin-NADP+ oxidoreductase
-
adrenodoxin reductase
-
-
-
-
DA1
-
-
-
-
Fd-NADP+ reductase
-
-
ferredoxin (flavodoxin)-NAD(P)H reductase
-
-
ferredoxin NADP+ reductase
-
-
ferredoxin-NAD(P)H reductase
-
-
ferredoxin-NADP oxidoreductase
-
-
-
-
ferredoxin-NADP reductase
-
-
-
-
Ferredoxin-NADP(+) reductase
-
-
-
-
ferredoxin-NADP(H) oxidoreductase
-
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ferredoxin-NADP(H) reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP-oxidoreductase
-
-
-
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ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
-
-
-
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ferredoxin-TPN reductase
-
-
-
-
ferredoxin: NADP(+) oxidoreductase
-
-
ferredoxin: NADP+ oxidoreductase
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ferredoxin:NADP+ oxidoreductase
-
-
-
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Flavodoxin reductase
-
-
-
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FLDR
-
-
-
-
FLXR
-
-
-
-
NADP:ferredoxin oxidoreductase
-
-
-
-
NADPH:ferredoxin oxidoreductase
-
-
-
-
NFR
-
-
-
-
reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
-
-
-
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reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
-
-
-
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TPNH-ferredoxin reductase
-
-
-
-
additional information
-
leaf-type, or chloroplast, or photosynthetic LFNR
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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 hide
56367-57-8
-
9029-33-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
-
-
-
-
r
NADPH + acceptor
NADP+ + reduced acceptor
show the reaction diagram
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
additional information
-
poor activity with NAD(H)
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
in the iron-sulfur center of ferredoxin
Iron
-
enzyme contains an [2Fe2S] cluster as prosthetic group involved in the reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 2',5'-diphosphate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
-
moderate NaCl concentrations less than 200 mM at pH 8.0 is more effective for enhancing enzyme activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.012
NADPH
0.0022 - 0.0024
reduced ferredoxin
additional information
additional information
-
stopped flow kinetic analysis
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
isozyme FNRI
6.76
isozyme FNRI
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
FNR is bound to thylakoid membranes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9SLP6_MAIZE
355
0
39323
TrEMBL
Chloroplast (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination and analysis of leaf enzyme, free or complexed with ferredoxin, and root enzyme at 2.2-2.6 and 1.7 A resolution, respectively
-
hanging drop vapor diffusion method, using 20% (w/v) PEG6000, 100 mM sodium cacodylate, pH 6.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E19C
-
site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview
E25C
-
site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview
E36C
-
site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview
additional information
-
introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant ferredoxin and Fd-NADP+ reductases from Escherichia coli strain BL21(DE3) the latter as homodimers, separation to monomers and crosslinking, further purification of crosslinked complexes by anion exchange chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of wild-type and mutant ferredoxin and Fd-NADP+ reductases in Escherichia coli strain BL21(DE3)
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expressed in Escherichia coli
expressed in Escherichia coli TG1 cells
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expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aliverti, A.; Faber, R.; Finnerty, C.M.; Ferioli, C.; Pandini, V.; Negri, A.; Karplus, P.A.; Zanetti, G.
Biochemical and crystallographic characterization of ferredoxin-NADP+ reductase from nonphotosynthetic tissues
Biochemistry
40
14501-14508
2001
Zea mays, Spinacia oleracea (P00455), Spinacia oleracea
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Karplus, P.A.; Faber, H.R.
Structural aspects of plant ferredoxin: NADP(+) oxidoreductases
Photosynth. Res.
81
303-315
2004
Trichormus variabilis, Capsicum annuum, Pisum sativum, Spinacia oleracea, Zea mays
Manually annotated by BRENDA team
Maeda, M.; Lee, Y.H.; Ikegami, T.; Tamura, K.; Hoshino, M.; Yamazaki, T.; Nakayama, M.; Hase, T.; Goto, Y.
Identification of the N- and C-terminal substrate binding segments of ferredoxin-NADP+ reductase by NMR
Biochemistry
44
10644-10653
2005
Zea mays
Manually annotated by BRENDA team
Lee, Y.H.; Tamura, K.; Maeda, M.; Hoshino, M.; Sakurai, K.; Takahashi, S.; Ikegami, T.; Hase, T.; Goto, Y.
Cores and pH-dependent dynamics of ferredoxin-NADP+ reductase revealed by hydrogen/deuterium exchange
J. Biol. Chem.
282
5959-5967
2007
Zea mays
Manually annotated by BRENDA team
Kimata-Ariga, Y.; Sakakibara, Y.; Ikegami, T.; Hase, T.
Electron transfer of site-specifically cross-linked complexes between ferredoxin and ferredoxin-NADP+ reductase
Biochemistry
49
10013-10023
2010
Zea mays
Manually annotated by BRENDA team
Mulo, P.
Chloroplast-targeted ferredoxin-NADP+ oxidoreductase (FNR): Structure, function and location
Biochim. Biophys. Acta
1807
927-934
2010
Arabidopsis thaliana (F4JZ46), Arabidopsis thaliana (Q8W493), Triticum aestivum (Q8RVZ8), Triticum aestivum (Q8RVZ9), Zea mays (Q9SLP6)
Manually annotated by BRENDA team
Dumit, V.I.; Essigke, T.; Cortez, N.; Ullmann, G.M.
Mechanistic insights into ferredoxin-NADP(H) reductase catalysis involving the conserved glutamate in the active site
J. Mol. Biol.
397
814-825
2010
Zea mays
Manually annotated by BRENDA team
Benz, J.P.; Lintala, M.; Soll, J.; Mulo, P.; Boelter, B.
A new concept for ferredoxin-NADP(H) oxidoreductase binding to plant thylakoids
Trends Plant Sci.
15
608-613
2010
Arabidopsis thaliana, Nicotiana tabacum, Spinacia oleracea, Zea mays
Manually annotated by BRENDA team
Lee, Y.H.; Ikegami, T.; Standley, D.M.; Sakurai, K.; Hase, T.; Goto, Y.
Binding energetics of ferredoxin-NADP+ reductase with ferredoxin and its relation to function
ChemBioChem
12
2062-2070
2011
Zea mays
Manually annotated by BRENDA team
Shinohara, F.; Kurisu, G.; Hanke, G.; Bowsher, C.; Hase, T.; Kimata-Ariga, Y.
Structural basis for the isotype-specific interactions of ferredoxin and ferredoxin NADP+ oxidoreductase an evolutionary switch between photosynthetic and heterotrophic assimilation
Photosynth. Res.
134
281-289
2017
Zea mays (B4G043)
Manually annotated by BRENDA team
Kinoshita, M.; Kim, J.Y.; Kume, S.; Lin, Y.; Mok, K.H.; Kataoka, Y.; Ishimori, K.; Markova, N.; Kurisu, G.; Hase, T.; Lee, Y.H.
Energetic basis on interactions between ferredoxin and ferredoxin NADP+ reductase at varying physiological conditions
Biochem. Biophys. Res. Commun.
482
909-915
2017
Zea mays
Manually annotated by BRENDA team
Kinoshita, M.; Kim, J.Y.; Kume, S.; Sakakibara, Y.; Sugiki, T.; Kojima, C.; Kurisu, G.; Ikegami, T.; Hase, T.; Kimata-Ariga, Y.; Lee, Y.H.
Physicochemical nature of interfaces controlling ferredoxin NADP+ reductase activity through its interprotein interactions with ferredoxin
Biochim. Biophys. Acta
1847
1200-1211
2015
Zea mays
Manually annotated by BRENDA team
Mulo, P.; Medina, M.
Interaction and electron transfer between ferredoxin-NADP+ oxidoreductase and its partners structural, functional, and physiological implications
Photosynth. Res.
134
265-280
2017
Nostoc sp. PCC 7119 (P21890), Zea mays (Q9SLP6)
Manually annotated by BRENDA team