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Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FKW6
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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
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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: Arabidopsis thaliana
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
FNR1
In Arabidopsis thaliana, two distinct chloroplast-targeted FNR isoforms, FNR1 and FNR2, are encoded by nuclear genes At5g66190 and At1g20020, respectively. In wild-type plants, both FNR isoforms exist partially in soluble form in the stroma and partially attached to the thylakoid membrane, as well as to the inner envelope membrane of the chloroplast.
LFNR1
isozyme, involved in linear electron transfer and thereby affects the function of the Calvin cycle
adrenodoxin reductase
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-
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DA1
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ferredoxin-NADP oxidoreductase
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ferredoxin-NADP reductase
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-
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Ferredoxin-NADP(+) reductase
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-
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ferredoxin-NADP+ oxidoreductase
ferredoxin-NADP-oxidoreductase
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ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
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ferredoxin-TPN reductase
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-
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ferredoxin:NADP+ oxidoreductase
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Flavodoxin reductase
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-
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FLDR
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-
-
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FLXR
-
-
-
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FNR
FNR2
NADP:ferredoxin oxidoreductase
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NADPH:ferredoxin oxidoreductase
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NFR
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reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
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reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
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TPNH-ferredoxin reductase
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additional information
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leaf-type, or chloroplast, or photosynthetic LFNR
FNR
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-
-
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FNR2
In Arabidopsis thaliana, two distinct chloroplast-targeted FNR isoforms, FNR1 and FNR2, are encoded by nuclear genes At5g66190 and At1g20020, respectively. In wild-type plants, both FNR isoforms exist partially in soluble form in the stroma and partially attached to the thylakoid membrane, as well as to the inner envelope membrane of the chloroplast.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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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
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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
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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-
-
r
oxidized 2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
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-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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-
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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-
-
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r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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-
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r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
FNR C-terminal domain harbors the NADP+ binding site
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r
additional information
?
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-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
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?
additional information
?
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FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
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?
additional information
?
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FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
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?
additional information
?
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the enzyme does not interact with Arabidopsis ferredoxin 1
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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 ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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-
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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-
-
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r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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-
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r
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tic62
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required for FNR binding to thylakoid membranes, FNR-binding motifs, overview
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TROL
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required for FNR binding to thylakoid membranes, FNR-binding motifs, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2000
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type and T-DNA insertion line fnr1 (lacking FNR1) and RNAi line fnr2 (lacking FNR2)
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
both FNR chloroplast isozyme genes are predominantly expressed in the rosette leaves
additional information
additional information
only minor amount of chloroplast isozyme FNR mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue
additional information
only minor amount of chloroplast isozyme FNR mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue
additional information
only minor amount of chloroplast isozyme FNR1 mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue
additional information
only minor amount of chloroplast isozyme FNR1 mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
In Arabidopsis thaliana, FNR1 is essential for the binding of FNR to the thylakoid membrane, hence in FNR1-lacking plant lines FNR2 can only be found in stroma.
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FNR occurs in stroma, at the inner envelope membrane, and bound to thylakoid membranes. Tic62 and TROL complexes are responsible for the major part of the thylakoid-bound pool of FNR
isozyme FNRI is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview
isozyme FNRII is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview
In Arabidopsis thaliana, FNR1 is essential for the binding of FNR to the thylakoid membrane, hence in FNR1-lacking plant lines FNR2 can only be found in stroma.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
FNR mediates the final step of photosynthetic electron flow by transferring electrons from ferredoxin to NADP+
metabolism
physiological function
additional information
metabolism
FNR mediates the final step of photosynthetic electron flow by transferring electrons from ferredoxin to NADP+
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
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the ferredoxin:ferredoxin-NADP+ oxidoreductase couple is an important mediator for these processes because it provides the transition from exclusively membrane-bound light reactions to the mostly stromal metabolic pathways
physiological function
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the enzyme has a major role in reduction of toxic nitrite in roots
physiological function
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the enzyme plays a central role in chloroplast redox metabolism. Thylakoid-bound enzyme activity decreases while excess soluble enzyme increases superoxide radical production in the light
additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery
additional information
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery
additional information
-
the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast. In Arabidopsis mutants completely devoid of FNR1 or FNR2 all high molecular weight FNR complexes are absent
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FNRL1_ARATH
360
0
40326
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
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LFNR1 is essential for the membrane attachment of LFNR2, strongly indicating the formation of a heterodimer
additional information
additional information
chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview
additional information
chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is neither phosphorylated nor glycosylated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
-
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
-
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
-
construction of in Arabidopsis mutants completely devoid of FNR1 or FNR2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisPur cobalt resin column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lintala, M.; Allahverdiyeva, Y.; Kidron, H.; Piippo, M.; Battchikova, N.; Suorsa, M.; Rintamaeki, E.; Salminen, T.A.; Aro, E.M.; Mulo, P.
Structural and functional characterization of ferredoxin-NADP+-oxidoreductase using knock-out mutants of Arabidopsis
Plant J.
49
1041-1052
2007
Arabidopsis thaliana (Q8W493), Arabidopsis thaliana (Q9FKW6), Arabidopsis thaliana
Lintala, M.; Allahverdiyeva, Y.; Kangasjaervi, S.; Lehtimaeki, N.; Keraenen, M.; Rintamaeki, E.; Aro, E.M.; Mulo, P.
Comparative analysis of leaf-type ferredoxin-NADP oxidoreductase isoforms in Arabidopsis thaliana
Plant J.
57
1103-1115
2009
Arabidopsis thaliana (Q8W493), Arabidopsis thaliana (Q9FKW6), Arabidopsis thaliana
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)
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
Lintala, M.; Schuck, N.; Thormhlen, I.; Jungfer, A.; Weber, K.; Weber, A.; Geigenberger, P.; Soll, J.; Blter, B.; Mulo, P.
Arabidopsis tic62 trol mutant lacking thylakoid-bound ferredoxin-NADP+ oxidoreductase shows distinct metabolic phenotype
Mol. Plant
7
45-57
2014
Arabidopsis thaliana
Koskela, M.M.; Dahlstroem, K.M.; Goni, G.; Lehtimaeki, N.; Nurmi, M.; Velazquez-Campoy, A.; Hanke, G.; Boelter, B.; Salminen, T.A.; Medina, M.; Mulo, P.
Arabidopsis FNRL protein is an NADPH-dependent chloroplast oxidoreductase resembling bacterial ferredoxin-NADP+ reductases
Physiol. Plant.
162
177-190
2018
Arabidopsis thaliana (Q9XI55)
Hachiya, T.; Ueda, N.; Kitagawa, M.; Hanke, G.; Suzuki, A.; Hase, T.; Sakakibara, H.
Arabidopsis root-type ferredoxin NADP(H) oxidoreductase 2 is involved in detoxification of nitrite in roots
Plant Cell Physiol.
57
2440-2450
2016
Arabidopsis thaliana
Lehtimaeki, N.; Koskela, M.M.; Dahlstroem, K.M.; Pakula, E.; Lintala, M.; Scholz, M.; Hippler, M.; Hanke, G.T.; Rokka, A.; Battchikova, n.; salminen, t.a.; mulo, p.
posttranslational modifications of ferredoxin-NADP+ oxidoreductase in Arabidopsis chloroplasts
Plant Physiol.
166
1764-1776
2014
Arabidopsis thaliana
Kozuleva, M.; Goss, T.; Twachtmann, M.; Rudi, K.; Trapka, J.; Selinski, J.; Ivanov, B.; Garapati, P.; Steinhoff, H.J.; Hase, T.; Scheibe, R.; Klare, J.P.; Hanke, G.T.
Ferredoxin NADP(H) oxidoreductase abundance and location influences redox poise and stress tolerance
Plant Physiol.
172
1480-1493
2016
Arabidopsis thaliana
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