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Information on EC 1.8.1.9 - thioredoxin-disulfide reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q39242
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1.8.1.9 thioredoxin-disulfide reductaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.8.1.9
- selenium
-
selenoproteins
- selenocysteine
- gsh
- peroxiredoxins
- dismutase
- catalase
- auranofin
- glutaredoxins
- trx1
-
selenoenzyme
- hydroperoxide
- peroxidases
- fad
- ribonucleotide
-
redox-active
- cisplatin
- dithiols
-
goldi
-
se-deficient
- dtnb
-
iodothyronine
-
flavoenzyme
- ebselen
-
redox-sensitive
-
selenium-containing
-
selenols
-
deiodinases
-
thiol-dependent
-
organoselenium
-
thioredoxin-like
-
selenium-deficient
-
se-dependent
-
n-heterocyclic
-
thioredoxin-dependent
- diselenide
-
redox-regulated
-
selenium-dependent
-
thiol-disulfide
-
thiol-based
- thioredoxin-1
- ask1
-
carbene
- 1-chloro-2,4-dinitrobenzene
- sulforaphane
-
secis
-
txnip
- trypanothione
- medicine
- analysis
- na2seo3
- agriculture
-
thioredoxin-interacting
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
thioredoxin reductase, trxr, trxr1, txnrd1, thioredoxin reductase 1, trxr2, txnrd2, thioredoxin reductase-1, thioredoxin reductase 2, nadph-dependent thioredoxin reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
general stress protein 35
-
-
-
-
GSP35
-
-
-
-
NADP-thioredoxin reductase
-
-
-
-
NADPH thioredoxin reductase C
NADPH-dependent thioredoxin reductase
NADPH-thioredoxin reductase
NADPH2:oxidized thioredoxin oxidoreductase
-
-
-
-
NTR
NTRC
reductase, thioredoxin
-
-
-
-
thioredoxin reductase (NADPH)
-
-
-
-
NADPH-thioredoxin reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9074-14-0
-
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-Cys peroxiredoxin + NADH
?
-
NADH is a poor electron donor for NTRC activity
-
-
?
2-Cys peroxiredoxin + NADPH
?
-
NTRC is able to conjugate NADPH thioredoxin reductase and thioredoxin activities for the efficient reduction of 2-Cys peroxiredoxin
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
-
-
-
?
CHLI-1 ATPase + NADPH + H+
CHLI-1 ATPase disulfide + NADP+
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant G47P + NADP+
Hordeum vulgare thioredoxin 2 mutant G47P disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
-
-
-
?
additional information
?
-
-
plants of the ntra ntrb knockout mutant are viable and fertile, although with a wrinkled seed phenotype, slower plant growth, and pollen with reduced fitness. Neither cytosolic nor mitochondrial NADPH-dependent thioredoxin reductases are essential in plants
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
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
additional information
?
-
-
plants of the ntra ntrb knockout mutant are viable and fertile, although with a wrinkled seed phenotype, slower plant growth, and pollen with reduced fitness. Neither cytosolic nor mitochondrial NADPH-dependent thioredoxin reductases are essential in plants
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00048
Arabidopsis thaliana thioredoxin 3
pH 7.5, temperature not specified in the publication
-
0.06
Hordeum vulgare thioredoxin 2
pH 7.5, temperature not specified in the publication
-
additional information
additional information
-
additionally to the Arabidopsis thaliana thioredoxin, several other thioredoxins have been tested, Km-values
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
Arabidopsis thaliana thioredoxin 3
pH 7.5, temperature not specified in the publication
-
8.5
Hordeum vulgare thioredoxin 2
pH 7.5, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12300
Arabidopsis thaliana thioredoxin 3
pH 7.5, temperature not specified in the publication
-
140
Hordeum vulgare thioredoxin 2
pH 7.5, temperature not specified in the publication
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
regulation of enzyme activity based on thiol-disulfide exchange is a regulatory mechanism in which the protein disulfide reductase activity of thioredoxins (TRXs) plays a central role. Plant chloroplasts are equipped with a complex set of up to 20 TRXs and TRX-like proteins, the activity of which is supported by reducing power provided by photosynthetically reduced ferredoxin (FDX) with the participation of a FDX-dependent TRX reductase (FTR). Therefore, the FDX-FTR-TRXs pathway allows the regulation of redox-sensitive chloroplast enzymes in response to light. In addition, chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. The NTRC gene encodes a polypeptide containing both NTR and TRX domains. NTRC is unique to oxygenic photosynthetic organisms. Both redox systems, NTRC and FDX-FTR-TRXs, participate in fine-tuning chloroplast performance in response to changes in light intensity. Participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase, in the control of the reducing activity of chloroplast TRXs as well as in the rapid oxidation of stromal enzymes upon darkness. Analysis of relationship of 2-Cys PRXs with NTRC and the FDX-FTR-TRXs redox systems for fine-tuning chloroplast performance in response to changes in light intensity and darkness, overview. The activity of thiol-dependent peroxidases (TPXs) relies on the disulfide reductase activity of NTRC, TRXs, and glutaredoxins (GRXs)
physiological function
additional information
NTRC can be considered as a TRX that bears its own NTR, which might explain the high catalytic efficiency of the enzyme. The catalytically active form of NTRC is a homodimer arranged in a head-to-tail conformation, which interacts with 2-Cys PRXs through the TRX domain with high affinity for NADPH
malfunction
-
in the absence of NTRC, imbalanced metabolic activities presumably modulate the chloroplast retrograde signals, leading to altered expression of nuclear genes and, ultimately, to the formation of the pleiotrophic phenotypes in ntrc mutant plants
malfunction
-
combined deficiencies of three thioredoxin m isoforms and NADPH-dependent thioredoxin reductase C (NTRC) leads to a cumulative decrease in leaf pigmentation, tetrapyrrole biosynthesis intermediate contents, 5-aminolevulinic acid synthesis rate, and Mg-protoporphyrin IX methyltransferase activity
malfunction
in plants with altered content of the NADPH-dependent chloroplast thioredoxin system, the strict correlation between lumenal pH and non-photochemical quenching is partially lost
malfunction
truncated polypeptides containing either the NTR or the TRX domain of NTRC showed that this novel enzyme could display both activities. Overexpression of 2-Cys PRXs, which has no significant effect in wild-type plants, resultes in further growth impairment in the ntrc mutant background (lacking individual TRXs), showing that the severity of the ntrc phenotype depends on 2-Cys PRXs levels. Very severe growth inhibition phenotypes of mutants combining the deficiencies of NTRC and TRXs f or x are also rescued by decreasing the contents of 2-Cys PRXs
physiological function
-
NTRC is the most important pathway for chloroplast 2-Cys peroxiredoxins reduction, probably the only one during the night
physiological function
-
NTRC regulates several key processes, including chlorophyll biosynthesis and the shikimate pathway, in chloroplasts. NTRC has a critical role in the regulation of photoperiod-dependent metabolic and developmental processes in Arabidopsis
physiological function
a double knockout mutant lacking NtrC and sulfiredoxin shows a phenotype similar to the NtrC mutant, while the sulfiredoxin mutant resembles wild-type plants. The deficiency of NtrC causes reduced overoxidation of 2-Cys peroxiredoxins, whereas the deficiency of sulfiredoxin has the opposite effect. The disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation. The overoxidation of chloroplast 2-Cys peroxiredoxins shows no circadian oscillation. The low level of 2-Cys peroxiredoxin overoxidation in the NtrC mutant is light dependent
physiological function
Arabidopsis thaliana NtrC knockout mutants show lower magnesium protoporphyrin IX and magnesium protoporphyrin IX monomethylester steady-state levels, the substrate and the product of protoporphyrin IX methyltransferase CHLM preceding MgPMME cyclase, while protoporphyrin IX strongly accumulates in mutant leaves after 5-aminolevulinic acid feeding. The mutant has a reduced capacity to synthesize 5-aminolevulinic acid and reduced CHLM activity compared with the wild-type. The contents of glutamyl-transfer RNA reductase1 and CHLM are reduced. NtrC physically interacts with glutamyl-transfer RNA reductase1 and CHLM. NtrC mutant plants contain partly oxidized CHLM, the wild-type has only reduced CHLM
physiological function
Arabidopsis thaliana plants lacking NtrC tolerate high light intensities, display drastically elevated non-photochemical quenching component qE, have larger trans-thylakoid pH differences and have 10fold higher zeaxanthin levels under low and medium light intensities. A double-knockout mutant, lacking additionally photosystem II component PsbS, is devoid of qE. This double mutant grows faster than the NtrC mutant and has a higher chlorophyll content. The photosystem II activity is partially restored, and linear electron transport rates under low and medium light intensities are twice as high as compared with plants lacking NtrC alone
physiological function
mutants lacking both NtrC and thioredoxin Trxs f, which participate in metabolic redox regulation, or, to a lower extent Trx x, which has antioxidant function, show severe growth-retarded phenotypes, decreased photosynthesis performance, and almost abolished light-dependent reduction of fructose-1,6-bisphosphatase. The combined deficiency of both redox systems provokes aberrant chloroplast ultrastructure. Both the NtrC-Trx f1f2 and NtrC-trx x mutants show high mortality at the seedling stage, which is overcome by the addition of an exogenous carbon source
physiological function
overexpression of isoform NTRC in Arabidopsis thaliana leads to a freezing and cold stress tolerance, whereas a knockout mutant shows a stress-sensitive phenotype. The recombinant NTRC proteins exhibits a cryoprotective activity for malate dehydrogenase and lactic dehydrogenase. Recombinant NTRC efficiently protect RNA and DNA from RNase A and metal catalyzed oxidation damage, respectively. The C-terminal thioredoxin domain is required for the nucleic acid-protein complex formation
physiological function
overexpression wild-type NtrC promotes plant growth by increasing leaf size and biomass yield of the rosettes. Complementation of the mutant with the full-length NtrC gene containing an active reductase but an inactive Trx domain, or vice versa, recovers wild-type chloroplast phenotype and, partly, rosette biomass production
physiological function
plants lacking functional NtrC show localized cell death accompanied by elevated accumulation of hydrogen peroxide in response to Pseudomonas syringae pathogens. The NtrC mutant shows enhanced bacterial growth and disease susceptibility of pathogens and elevated jasmonic acid-mediated signaling pathways in response to Pseudomonas syringae pathogens
physiological function
the enhanced NtrC transcript expression upon methyl viologen treamtment confers oxidative stress tolerance. Overexpressing plants show extreme drought tolerance with lower water loss compared to wild-type and NtrC mutant strains. Drought-responsive genes such as RD29A and DREB2A are enhanced in overexpressing strains by drought, compared to wild-type and NtrC mutant strains
physiological function
the NtrC-dependent redox regulation of CHLI-1 ATPase contributes to the chlorophyll-deficient phenotype of NtrC mutants
physiological function
chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. Redox regulation is an additional layer of control of the signaling function of the chloroplast. Redox regulation based on dithiol-disulfide interchange constitutes an essential regulatory mechanism that allows the rapid adaptation of chloroplast metabolism to light
physiological function
redox regulation in heterotrophic organisms relies on NADPH, thioredoxins, and an NADPH-dependent TRX reductase (NTR). NTRC-dependent regulation of 2-Cys peroxiredoxin (PRX) is critical for optimal function of the photosynthetic apparatus
physiological function
the enzyme (NTRC) plays a crucial role in the activation of the NDH-dependent electron flow in darkness (chlororespiration) and during dark to light transitions. The enzyme stimulates the activity of NDH-dependent cyclic electron flow and is involved in the regulation of generation of proton motive force, thylakoid conductivity to protons, and redox balance between the thylakoid electron transfer chain and the stroma during changes in light conditions
physiological function
the NADPH-dependent chloroplast thioredoxin system (NTRC) contributes to downregulation of a slow-relaxing constituent of NPQ, whose induction is independent of lumenal acidification. Overexpression of NTRC enhances the ability to adjust the excitation balance between photosystem II (PSII) and photosystem I (PSI), and improves the ability to oxidize the electron transfer chain during changes in light conditions
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). TRXB2_ARATH
383
0
40635
Swiss-Prot
Chloroplast (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
153000
-
low-molecular-mass form of NTRC observed in the presence of NADPH or dithiothreitol, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
NTRC can be considered as a TRX that bears its own NTR, the catalytically active form of NTRC is a homodimer arranged in a head-to-tail conformation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of the structure of the NtrC dimer, extensive interactions between the Ntr domains and the Trx domains may stabilize the dimeric structure. A long linker region between the Ntr domain and Trx domain allows flexibility for the position of the Trx domain in the dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A164G/R183F
-
the mutant shows reduced activity but is still able to dimerize though with an increase in intermediary forms
A164G/V182E
-
the mutant shows increased activity compared to the wild type enzyme
A164G/V182E/R183F
-
the mutant shows reduced activity compared to the wild type enzyme but is still able to dimerize though with an increase in intermediary forms
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of NTRC enzyme tagged at the C-terminus with nine copies of the myc epitope (9×myc), six histidine residues (6×His), a 3C protease cleavage site (3C), and two copies of the protein A IgG-binding domain
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is affected by alternative splicing resulting in a transcript with premature stop codon, which would produce a truncated form of the enzyme. The standard splicing/alternative splicing (SS/AS) transcripts ratio is higher in photosynthetic tissues from Arabidopsis thaliana, Brachypodium distachyon and Solanum lycopersicum, in line with the higher content of the NtrC polypeptide in these tissues
methyl viologen treatment leads to 2fold induction of transcript expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacquot, J.P.; Rivera-Madrid, R.; Marinho, P.; Kollarova, M.; Le Marechal, P.; Miginiac-Maslow, M.; Meyer, Y.
Arabidopsis thaliana NADPH thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli
J. Mol. Biol.
235
1357-1363
1994
Arabidopsis thaliana
Reichheld, J.P.; Meyer, E.; Khafif, M.; Bonnard, G.; Meyer, Y.
AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana
FEBS Lett.
579
337-342
2005
Arabidopsis thaliana (Q39242), Arabidopsis thaliana (Q39243), Arabidopsis thaliana
Reichheld, J.P.; Khafif, M.; Riondet, C.; Droux, M.; Bonnard, G.; Meyer, Y.
Inactivation of thioredoxin reductases reveals a complex interplay between thioredoxin and glutathione pathways in Arabidopsis development
Plant Cell
19
1851-1865
2007
Arabidopsis thaliana
Kirchsteiger, K.; Pulido, P.; Gonzalez, M.; Cejudo, F.J.
NADPH thioredoxin reductase C controls the redox status of chloroplast 2-Cys peroxiredoxins in Arabidopsis thaliana
Mol. Plant
2
298-307
2009
Arabidopsis thaliana
Perez-Ruiz, J.M.; Gonzalez, M.; Spinola, M.C.; Sandalio, L.M.; Cejudo, F.J.
The quaternary structure of NADPH thioredoxin reductase C is redox-sensitive
Mol. Plant
2
457-467
2009
Arabidopsis thaliana
Lepistoe, A.; Kangasjaervi, S.; Luomala, E.M.; Brader, G.; Sipari, N.; Keraenen, M.; Keinaenen, M.; Rintamaeki, E.
Chloroplast NADPH-thioredoxin reductase interacts with photoperiodic development in Arabidopsis
Plant Physiol.
149
1261-1276
2009
Arabidopsis thaliana, Arabidopsis thaliana ecotype Col-0
Jacquot, J.P.; Eklund, H.; Rouhier, N.; Schuermann, P.
Structural and evolutionary aspects of thioredoxin reductases in photosynthetic organisms
Trends Plant Sci.
14
336-343
2009
Arabidopsis thaliana
Moon, J.C.; Lee, S.; Shin, S.Y.; Chae, H.B.; Jung, Y.J.; Jung, H.S.; Lee, K.O.; Lee, J.R.; Lee, S.Y.
Overexpression of Arabidopsis NADPH-dependent thioredoxin reductase C (AtNTRC) confers freezing and cold shock tolerance to plants
Biochem. Biophys. Res. Commun.
463
1225-1229
2015
Arabidopsis thaliana (O22229), Arabidopsis thaliana
Toivola, J.; Nikkanen, L.; Dahlstroem, K.M.; Salminen, T.A.; Lepistoe, A.; Vignols, H.F.; Rintamaeki, E.
Overexpression of chloroplast NADPH-dependent thioredoxin reductase in Arabidopsis enhances leaf growth and elucidates in vivo function of reductase and thioredoxin domains
Front. Plant Sci.
4
389
2013
Arabidopsis thaliana (O22229)
Puerto-Galan, L.; Perez-Ruiz, J.M.; Guinea, M.; Cejudo, F.J.
The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts
J. Exp. Bot.
66
2957-2966
2015
Arabidopsis thaliana (O22229), Arabidopsis thaliana
Kim, M.; Khaleda, L.; Jung, I.; Kim, J.; Lee, S.; Cha, J.; Kim, W.
Overexpression of chloroplast-localized NADPH-dependent thioredoxin reductase C (NTRC) enhances tolerance to photo-oxidative and drought stresses in Arabidopsis thaliana
J. Plant Biol.
60
175-180
2017
Arabidopsis thaliana (O22229)
-
Perez-Ruiz, J.; Guinea, M.; Puerto-Galan, L.; Cejudo, F.
NADPH thioredoxin reductase C is involved in redox regulation of the Mg-chelatase I subunit in Arabidopsis thaliana chloroplasts
Mol. Plant
7
1252-1255
2014
Arabidopsis thaliana (O22229), Arabidopsis thaliana
Ishiga, Y.; Ishiga, T.; Ikeda, Y.; Matsuura, T.; Mysore, K.
NADPH-dependent thioredoxin reductase C plays a role in nonhost disease resistance against Pseudomonas syringae pathogens by regulating chloroplast-generated reactive oxygen species
PeerJ
4
e1938
2016
Arabidopsis thaliana (O22229)
Naranjo, B.; Mignee, C.; Krieger-Liszkay, A.; Hornero-Mendez, D.; Gallardo-Guerrero, L.; Cejudo, F.J.; Lindahl, M.
The chloroplast NADPH thioredoxin reductase C, NTRC, controls non-photochemical quenching of light energy and photosynthetic electron transport in Arabidopsis
Plant Cell Environ.
39
804-822
2016
Arabidopsis thaliana (O22229), Arabidopsis thaliana
Richter, A.S.; Peter, E.; Rothbart, M.; Schlicke, H.; Toivola, J.; Rintamaeki, E.; Grimm, B.
Posttranslational influence of NADPH-dependent thioredoxin reductase C on enzymes in tetrapyrrole synthesis
Plant Physiol.
162
63-73
2013
Arabidopsis thaliana (O22229)
Ojeda, V.; Perez-Ruiz, J.M.; Gonzalez, M.; Najera, V.A.; Sahrawy, M.; Serrato, A.J.; Geigenberger, P.; Cejudo, F.J.
NADPH thioredoxin reductase C and thioredoxins act concertedly in seedling development
Plant Physiol.
174
1436-1448
2017
Arabidopsis thaliana (O22229)
Najera, V.A.; Gonzalez, M.C.; Perez-Ruiz, J.M.; Cejudo, F.J.
An event of alternative splicing affects the expression of the NTRC gene, encoding NADPH-thioredoxin reductase C, in seed plants
Plant Sci.
258
21-28
2017
Solanum lycopersicum, Brachypodium distachyon (A0A0Q3NCX3), Arabidopsis thaliana (O22229)
Kirkensgaard, K.; Hagglund, P.; Shahpiri, A.; Finnie, C.; Henriksen, A.; Svensson, B.
A novel twist on molecular interactions between thioredoxin and nicotinamide adenine dinucleotide phosphate-dependent thioredoxin reductase
Proteins
82
607-619
2014
Hordeum vulgare subsp. vulgare (A9LN30), Arabidopsis thaliana (Q39243), Arabidopsis thaliana
Gonzalez, M.; Delgado-Requerey, V.; Ferrandez, J.; Serna, A.; Cejudo, F.J.
Insights into the function of NADPH thioredoxin reductase C (NTRC) based on identification of NTRC-interacting proteins in vivo
J. Exp. Bot.
70
5787-5798
2019
Arabidopsis thaliana (O22229), Arabidopsis thaliana
Nikkanen, L.; Guinea Diaz, M.; Toivola, J.; Tiwari, A.; Rintamaeki, E.
Multilevel regulation of non-photochemical quenching andstate transitions by chloroplast NADPH-dependent thioredoxin reductase
Physiol. Plant.
166
211-225
2019
Arabidopsis thaliana (O22229)
Nikkanen, L.; Toivola, J.; Trotta, A.; Diaz, M.G.; Tikkanen, M.; Aro, E.M.; Rintamaeki, E.
Regulation of cyclic electron flow by chloroplast NADPH-dependent thioredoxin system
Plant Direct
2
e00093
2018
Arabidopsis thaliana (O22229)
Da, Q.; Wang, P.; Wang, M.; Sun, T.; Jin, H.; Liu, B.; Wang, J.; Grimm, B.; Wang, H.B.
Thioredoxin and NADPH-dependent thioredoxin reductase C regulation of tetrapyrrole biosynthesis
Plant Physiol.
175
652-666
2017
Arabidopsis thaliana
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