1.18.1.2: ferredoxin-NADP+ reductase
This is an abbreviated version!
For detailed information about ferredoxin-NADP+ reductase, go to the full flat file.
Word Map on EC 1.18.1.2
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1.18.1.2
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nitrate
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ferredoxins
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denitrification
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denitrify
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reductases
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heme
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fad
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spinach
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chloroplast
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copper
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ammonia
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nitrous
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flavin
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dissimilatory
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photosystems
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flavodoxins
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denitrificans
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alcaligenes
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paracoccus
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n2o
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anabaena
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copper-containing
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thylakoids
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anammox
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p450scc
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semiquinone
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diaphorase
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viologen
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azurins
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ferredoxin-dependent
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stutzeri
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plant-type
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achromobacter
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flavoenzymes
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electron-transfer
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ammonia-oxidizing
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plastocyanin
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dinitrogen
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photoreduction
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gogat
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pregnenolone
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nitrate-induced
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xylosoxidans
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photoreduced
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wolinella
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isoalloxazine
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nitrate-reducing
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biotechnology
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nitrosomonas
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deoxyhemoglobin
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agriculture
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single-electron
- 1.18.1.2
- nitrate
- ferredoxins
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denitrification
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denitrify
- reductases
- heme
- fad
- spinach
- chloroplast
- copper
- ammonia
-
nitrous
- flavin
-
dissimilatory
- photosystems
- flavodoxins
- denitrificans
- alcaligenes
- paracoccus
- n2o
- anabaena
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copper-containing
- thylakoids
-
anammox
- p450scc
- semiquinone
- diaphorase
- viologen
- azurins
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ferredoxin-dependent
- stutzeri
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plant-type
- achromobacter
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flavoenzymes
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electron-transfer
-
ammonia-oxidizing
- plastocyanin
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dinitrogen
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photoreduction
- gogat
- pregnenolone
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nitrate-induced
- xylosoxidans
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photoreduced
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wolinella
- isoalloxazine
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nitrate-reducing
- biotechnology
- nitrosomonas
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deoxyhemoglobin
- agriculture
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single-electron
Reaction
2 reduced ferredoxin
+
Synonyms
ABO_0145, adrenodoxin reductase, AnFNR, BsFNR, CT1512, cytochrome b6f -associated ferredoxin:NADP+ oxidoreductase, DA1, EC 1.6.7.1, EC 1.6.99.4, Fd-NADP+ reductase, ferredoxin (flavodoxin)-(reduced) nicotinamide adenine dinucleotide phosphate reductase, ferredoxin (flavodoxin)-NAD(P)H reductase, ferredoxin (flavodoxin)-NADP(H) reductase, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin NADP oxidoreductase, ferredoxin NADP reductase, ferredoxin NADP(H) oxidoreductase, ferredoxin NADP+ oxidoreductase, ferredoxin NADP+ reductase, ferredoxin nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-NAD(P)+ oxidoreductase, ferredoxin-NAD(P)+ reductase, ferredoxin-NAD(P)H reductase, ferredoxin-NADP oxidoreductase, ferredoxin-NADP reductase, Ferredoxin-NADP(+) reductase, ferredoxin-NADP(H) oxidoreductase, ferredoxin-NADP(H) reductase, ferredoxin-NADP+ oxidoreductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+-oxidoreductase, ferredoxin-NADP+-reductase, ferredoxin-NADP-oxidoreductase, ferredoxin-NADP-reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase, ferredoxin-TPN reductase, ferredoxin: NADP(+) oxidoreductase, ferredoxin: NADP+ oxidoreductase, ferredoxin:NADP oxidoreductase, ferredoxin:NADP(+) oxidoreductase, ferredoxin:NADP(H) oxidoreductase, ferredoxin:NADP(H) oxidoreductase 2, ferredoxin:NADP+ oxidoreductase, ferredoxin:NADP+ reductase, ferredoxin:NADPH oxidoreductase, ferric reductase, Flavodoxin reductase, FLDR, FLXR, FNR, FNR-A, FNR-B, FNR1, FNR2, FNRII, FNRL, FNRS, FPR, FprA, FprB, Fprs, LFNR1, LFNR2, mitochondrial-type ferredoxin:NADP+ reductase, More, mtFNR, NADH-dependent reduced ferredoxin:NADP oxidoreductase, NADP:ferredoxin oxidoreductase, NADPH ferredoxin reductase, NADPH-dependent ferredoxin reductase, NADPH:ferredoxin oxidoreductase, NfnAB, NfnIII, NFR, PETH, PfFNR, pFNR, photosynthetic ferredoxin NADP+ oxidoreductase, photosynthetic FNR, plastidic-type ferredoxin-NADP+ reductase, PP4_41290, RcFPR, reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate, RFNR2, ST2133, TgFNR, TPNH-ferredoxin reductase, YumC
ECTree
1.18.1.2 ferredoxin-NADP+ reductaseAdvanced search results
results (
results (Cofactor
Cofactor on EC 1.18.1.2 - ferredoxin-NADP+ reductase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
NAD(P)H
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NADPH is absolutely preferred over NADH by the wild-type isozymes
[2Fe-2S] cluster
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iron-sulfur cluster reconstitution after enzyme purification in 100 mM Tris-HCl, pH 7.5, containing 8 mM DTT, 0.01 mM FAD, 2 mM cysteine, and 1.5 mM FeSO4 at room temperature for 1 h under strictly anaerobic conditions. Binding of FAD and the iron-sulfur clusters in the NfnAB complex
[4Fe-4S] cluster
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iron-sulfur cluster reconstitution after enzyme purification in 100 mM Tris-HCl, pH 7.5, containing 8 mM DTT, 0.01 mM FAD, 2 mM cysteine, and 1.5 mM FeSO4 at room temperature for 1 h under strictly anaerobic conditions. The proximal [4Fe-4S] cluster is embedded into a rather hydrophilic pocket, and the irons are ligated to three cysteines (Cys51, Cys90, and Cys96) and Glu117. Binding of FAD and the iron-sulfur clusters in the NfnAB complex
FAD
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in contrast to stromal reductase, the solubilized and purified membrane-bound enzyme contains no FAD
FAD
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extended conformation, interaction via Tyr96, direct electron transfer between FAD and ferredoxin [2Fe2S] center, modeling of conformation of C4alpha polypeptide backbone and FAD
FAD
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extended conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
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folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
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folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
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involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions
FAD
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involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions
FAD
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involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions
FAD
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involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions
FAD
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noncovalently bound prosthetic group, binding domain structure, ferredoxin binds to the concave region of the FAD domain
FAD
prosthetic group, tightly bound, can be released by heat denaturation
FAD
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structure contains two domains harboring FAD and NAD(P)H binding sites
FAD
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FAD is reduced rapidly and completely when the enzyme reacts with NADPH, while in contrast, addition of NADH results in very slow and inefficient reduction
FAD
BsFNR features two distinct binding domains for FAD and NADPH, binding structure, overview. A unique C-terminal extension covers the re-face of the isoalloxazine moiety of FAD. Tyr50 in the FAD-binding region and His324 in the Cterminal extension stack on the si- and re-faces of the isoalloxazine ring of FAD, respectively
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
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
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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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
the high stability of the enzyme might be due to robust interactions between the FAD and the NADP+ domains of the protein
FAD
reduction of the FAD moiety of phenylglyoxal-modified FNR by laser-generated 5-deazariboflavin semiquinone occurrs with a second-order rate constant 2.5fold smaller than that obtained for reduction of native FNR
FAD
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a-FAD and b-FAD, binding of FAD and the iron-sulfur clusters in the NfnAB complex, overview
FAD
flavin adenine dinucleotide prosthetic group, the FAD prosthetic group is noncovalently bound in the open conformation. The fluorescence intensity of the protein-bound FAD is influenced by its environment. The fluorescence emissions of enzyme mutants Y50G and Y50S enzymes increase six to sevenfold compared with that of free FAD, whereas the fluorescence emission of wild-type and Y50W enzymes is efficiently quenched to below 3% and 9% of that of free FAD. ENzyme residue Tyr50 plays an important role to stabilize the FAD prosthetic group
FAD
flavoprotein, analysis of specific interactions between FAD and the surrounding amino acids, overview
Ferredoxin
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[2Fe2S] cluster containing, ferredoxin I and II, and ferredoxin I mutants, the latter lacking the Arg39-Glu28 residues being essential for efficient electron transfer between the cofactor and the enzyme, the Fd I Q39R/S28E mutant is unstable and rapidly loose the [2Fe2S] cluster, the mutant shows 5.5fold reduced electron transfer rates compared to Fd I, ferredoxin II mutant D64N is about half as efficient as cofactor as the wild-type ferredoxin I and II are
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FMN
activates. Vmax is 1.38 and 21.8 U/mg (at 70°C) in the absence and presence of 1 mM FMN
NAD+
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enzyme reduces NADP+ and NAD+, specific for NADP+ reduction under physiological conditions
NADH
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structure contains two domains harboring FAD and NAD(P)H binding sites
NADP+
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reductase is covalently cross linked to Azotobacter vinelandii flavodoxin
NADP+
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enzyme reduces NADP+ and NAD+, specific for NADP+ reduction under physiological conditions
NADP+
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binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADP+
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binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADP+
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binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview
NADP+
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binding structure, binding causes conformational changes in the enzyme and creation of a new binding pocket near the FAD binding site
NADP+
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interaction with the enzyme, complex structure, specificity-determining structures, overview
NADP+
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interaction with the enzyme, complex structure, specificity-determining structures, overview
NADP+
Kd value 0.222 mM, coenzyme docking occurrs through the 2'-P-AMP moiety
NADPH
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binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADPH
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binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADPH
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binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview
NADPH
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structure contains two domains harboring FAD and NAD(P)H binding sites
additional information
the coenzyme specificity determining structures are located in the 2'-phosphate NADP+ and pyrophosphate binding region of amino acid residues 155-160, 261-268, and S233, R224, R233, and Y235, coenzyme binding causes structural rearrangements of the protein backbone, binding and interaction mechanism with the enzyme, overview
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additional information
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the structure of NfnAB reveals an electron transfer route including the a-FAD, the [2Fe-2S] cluster of NfnA and the b-FAD, and the two [4Fe-4S] clusters of NfnB. Ferredoxin is presumably docked onto NfnB close to the [4Fe-4S] cluster distal to b-FAD. NAD(H) binds to a-FAD and NADP(H) consequently to b-FAD, which is positioned in the center of the NfnAB complex and the site of electron bifurcation. Arg187 is hydrogen-bonded to N5 and O4 of the bifurcating b-FAD and might play a key role in adjusting a low redox potential of the FADH*/FAD pair required for ferredoxin reduction. Proposed mechanism of FAD-coupled electron bifurcation by NfnAB, overview
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