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ferredoxin-NADP+ oxidoreductase
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adrenodoxin reductase
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ferredoxin (flavodoxin)-NAD(P)H reductase
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ferredoxin NADP+ reductase
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ferredoxin-NAD(P)H reductase
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ferredoxin-NADP oxidoreductase
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ferredoxin-NADP reductase
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Ferredoxin-NADP(+) reductase
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ferredoxin-NADP(H) oxidoreductase
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ferredoxin-NADP(H) reductase
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ferredoxin-NADP+ reductase
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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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ferredoxin: NADP(+) oxidoreductase
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ferredoxin: NADP+ oxidoreductase
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ferredoxin:NADP+ oxidoreductase
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Flavodoxin reductase
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NADP:ferredoxin oxidoreductase
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NADPH:ferredoxin oxidoreductase
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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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2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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r
NADPH + acceptor
NADP+ + reduced acceptor
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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
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reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
additional information
?
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2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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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
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction
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reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues
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reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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responsible for NADPH generation
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reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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structure of the ferredoxin-enzyme complex, ferredoxin binds to the concave region of the FAD domain, overview, release of oxidized ferredoxin is rate-limiting
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r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting
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reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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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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enzyme has also NADPH-cytochrome c reductase activity
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additional information
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enzyme has also NADPH-diaphorase activity
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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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the enzyme also shows NADPH-dependent cyt c reductase activity
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2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
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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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r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
additional information
?
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reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction
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r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues
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r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
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responsible for NADPH generation
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r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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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 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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poor activity with NAD(H)
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FAD
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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
FAD
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FAD
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binding domain structure, structure-function relationship
FAD
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noncovalently bound prosthetic group
FAD
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noncovalently bound prosthetic group, binding domain structure, ferredoxin binds to the concave region of the FAD domain
FAD
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noncovalently bound, the flavin can adopt three different redox forms as the oxidized quinone form FAD, the one-electron reduced semiquinone radical form FADHradical, and the fully reduced quinol form FADH2
FAD
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one molecule of noncovalently bound
NADP+
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NADP+
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binding domain structure, binding mechanism
NADP+
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binding domain structure, structure-function relationship
NADPH
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binding domain structure, binding mechanism
NADPH
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binding domain structure, structure-function relationship
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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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ferredoxin and Fd-NADP+ reductase are redox partners responsible for the conversion between NADP+ and NADPH in the plastids of photosynthetic organisms
physiological function
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in chloroplasts and cyanobacteria, FNR provides the NADPH necessary for photosynthetic CO2 assimilation
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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ferredoxin-ferredoxin reductase binding is accompanied by endothermic reactions and driven by the entropy gain. Increases in the conformational entropy of the ferredoxin-ferredoxin reductase complex contribute largely to stabilizing the complex. Ferredoxin binding leads to both structural stiffening and softening of ferredoxin reductase. Enhanced ferredoxin reductase backbone fluctuations suggest favorable contributions to the net conformational entropy. Relatively large-scale motions of the C-terminus, a gatekeeper for interactions of NADP(H), are quenched in the closed form, thereby facilitating exit of NADP(H)
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
additional information
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introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins results in 13 different Fd-FNR cross-linked complexes displaying a broad range of activity to catalyze the NADPH-dependent cytochrome c reduction
additional information
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the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast
additional information
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titration behaviour of Glu312, overview
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda