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
-
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
-
electron-transfer
-
ammonia-oxidizing
-
plastocyanin
-
dinitrogen
-
photoreduction
-
gogat
-
pregnenolone
-
nitrate-induced
-
xylosoxidans
-
photoreduced
-
wolinella
-
isoalloxazine
-
nitrate-reducing
-
biotechnology
-
nitrosomonas
-
deoxyhemoglobin
-
agriculture
-
single-electron
- 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
-
electron-transfer
-
ammonia-oxidizing
- plastocyanin
-
dinitrogen
-
photoreduction
- gogat
- pregnenolone
-
nitrate-induced
- xylosoxidans
-
photoreduced
-
wolinella
- isoalloxazine
-
nitrate-reducing
- biotechnology
- nitrosomonas
-
deoxyhemoglobin
- agriculture
-
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 (Substrates Products
Substrates Products on EC 1.18.1.2 - ferredoxin-NADP+ reductase
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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
1,4-dioxo-2-(trifluoromethyl)-1lambda5,4lambda5-quinoxaline + NADPH + H+
? + NADP+
-
-
-
?
1,4-dioxo-7-(trifluoromethoxy)-1lambda5,2,4lambda5-benzotriazin-3-amine + NADPH + H+
? + NADP+
-
-
-
?
2 oxidized Fdx2 + NADPH + H+
2 reduced Fdx2 + NADP+
Fdx2 i.e. Chlamydomonas reinhardtii plant-type isoform ferredoxin 2
-
-
?
2 reduced ferredoxin + NAD+
2 oxidized ferredoxin + NADH + H+
NAD+ is a poor substrate
-
-
?
2,5-dimethyl-1,4-benzoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.07 V
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
?
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride + NADPH
?
-
-
-
?
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride + NADPH
? + NADP+
-
-
-
?
2-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.41 V
-
-
?
2-methyl-1,4-benzoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential 0.01 V
-
-
?
2-methyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.20 V
-
-
?
2-methyl-3-glutathionyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.16 V
-
-
?
2-methyl-3-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.46 V
-
-
?
2-methyl-5-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.16 V
-
-
?
3-amino-1,4-dioxo-1lambda5,4lambda5-quinoxaline-2-carbonitrile + NADPH + H+
? + NADP+
-
-
-
?
5,8-dihydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.11 V
-
-
?
5-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.09 V
-
-
?
9,10-phenanthrenequinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.12 V
-
-
?
aclacinomycin A + NADP+
7-deoxyaklavinone + NADPH
-
under anaerobic conditions
-
-
?
daunomycin + NADP+
7-deoxydaunomycinone + NADPH
-
under anaerobic conditions
-
-
?
daunorubicin + NADP+
? + NADPH + H+
-
single electron reduction potential -0.34 V
-
-
?
dibromothymoquinone + NADPH
? + NADP+
-
diaphorase activity, no direct involvement of thiol or amino groups in the reaction
-
-
?
Fe(III)-diethylenetriamine-N,N,N',N'',N''-pentaacetic acid + NADPH + H+
Fe(II) + diethylenetriamine-N,N,N',N'',N''-pentaacetic acid + NADP+
highest activity
-
-
?
Fe(III)-nitrilotriacetic acid + NADPH + H+
Fe(II) + nitrilotriacetic acid + NADP+
-
-
-
?
ferricyanide + NADP+
? + NADPH + H+
-
single electron acceptor, single electron reduction potential 0.41 V
-
-
?
Fe[EDTA]- + NADP+
? + NADPH + H+
-
single electron acceptor, single electron reduction potential 0.12 V
-
-
?
menogarol + NADP+
7-deoxynogarol + NADPH
-
under anaerobic conditions
-
-
?
methyl (1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)carbamate + NADPH + H+
? + NADP+
-
-
-
?
methylviologen + NADP+
? + NADPH + H+
-
single electron acceptor, single electron reduction potential -0.44 V
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)-1,1,1-trifluoromethanesulfonamide + NADPH + H+
? + NADP+
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)acetamide + NADPH + H+
? + NADP+
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)methanesulfonamide + NADPH + H+
? + NADP+
-
-
-
?
N-(1-oxo-1lambda5,2,4-benzotriazin-3-yl)acetamide + NADPH + H+
? + NADP+
-
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
NADPH + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride
NADP+ + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride
-
-
-
?
NADPH + FAD
NADP+ + reduced FAD
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
r
nogalamycin + NADP+
7-deoxynogalarol + NADPH
-
under anaerobic conditions
-
-
?
oxidized 2,3-bis(2-methoxy-4-nitro-5-sulfophenyl)-2H-tetrazolium-5-carboxanilide + NADPH
reduced 2,3-bis(2-methoxy-4-nitro-5-sulfophenyl)-2H-tetrazolium-5-carboxanilide + NADP+ + H+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADP+
reduced 2,6-dichlorophenolindophenol + NADPH
-
diaphorase activity
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
very slow and inefficient reaction
-
-
?
oxidized ferredoxin + NADH + cytochrome c
reduced ferredoxin + NAD+ + reduced cytochrome c
-
-
-
-
r
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
oxidized ferredoxin II mutant D64N + NADPH + H+
reduced ferredoxin II mutant D64N + NADP+
-
-
-
-
r
oxidized ferredoxin II mutant Q39R/S28E + NADPH + H+
reduced ferredoxin mutant Q39R/S28E + NADP+
-
-
-
-
r
oxidized iodonitrotetrazolium violet + NADPH
reduced iodonitrotetrazolium violet + NADP+
-
-
-
-
?
oxidized rubredoxin + NADP+
reduced rubredoxin + NADPH
-
Clostridium pasteurianum rubredoxin
-
-
?
plastoquinone + NADPH
? + NADP+
-
plastoquinones with different length of side chains from spinach, preference for short chain substrate, reaction proceeds via a FMN and a semiquinone intermediate, incorporation of the substrate into sodium cholate micelles is required for activity, micelles structure scheme
-
-
?
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone + NADP+ + H+
oxidized 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone + NADPH
-
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
oxidized 2,6-dichlorophenolindophenol + NADPH
reduced cytochrome c + NADP+
oxidized cytochrome c + NADPH + H+
-
-
-
?
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH
-
the rate of NADH oxidation by FNR is lower than that with NADPH
-
-
r
reduced ferredoxin II + NADP+
oxidized ferredoxin II + NADPH + H+
-
-
-
-
r
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
r
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
r
reduced flavodoxin mutant I59A + NADP+
oxidized flavodoxin mutant I59A + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant I59A/I92A + NADP+
oxidized flavodoxin mutant I59A/I92A + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant I59E + NADP+
oxidized flavodoxin mutant I59E + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant I59E/I92E + NADP+
oxidized flavodoxin mutant I59E/I92E + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant I92A + NADP+
oxidized flavodoxin mutant I92A + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant I92E + NADP+
oxidized flavodoxin mutant I92E + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant W57E + NADP+
oxidized flavodoxin mutant W57E + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant W57K + NADP+
oxidized flavodoxin mutant W57K + NADPH + H+
-
-
-
-
r
reduced flavodoxin mutant W57R + NADP+
oxidized flavodoxin mutant W57R + NADPH + H+
-
-
-
-
r
reduced iodonitrotetrazolium violet + NADP+
oxidized iodonitrotetrazolium violet + NADPH + H+
-
-
-
-
r
tetramethyl-1,4-benzoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.26 V
-
-
?
tirapazamine + NADPH + H+
1,2,4-benzotriazin-3-amine + 1-oxo-1lambda5,2,4-benzotriazin-3-amine + NADP+
-
-
-
?
1,4-benzoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential 0.09 V
-
-
?
1,4-benzoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential 0.09 V
-
-
?
1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.15 V
-
-
?
1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.15 V
-
-
?
1,8-dihydroxy-9,10-anthraquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.325 V
-
-
?
1,8-dihydroxy-9,10-anthraquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.325 V
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
high diaphorase activity
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
diaphorase activity
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
best substrate
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
diaphorase reaction
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
diaphorase reaction
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
i.e. K3Fe(CN)6, diaphorase activity
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
?
2 ferrocytochrome c + NAD+ + H+
2 ferricytochrome c + NADH
NADH, poor substrate
-
-
?
2 ferrocytochrome c + NAD+ + H+
2 ferricytochrome c + NADH
NADH, poor substrate
-
-
?
2 oxidized ferredoxin + NADH + H+
2 reduced ferredoxin + NAD+
NADH, poor substrate
-
-
?
2 oxidized ferredoxin + NADH + H+
2 reduced ferredoxin + NAD+
NADH, poor substrate
-
-
?
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
-
-
-
r
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
-
-
-
r
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
-
-
-
r
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
-
-
-
-
r
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
-
complete reversibility of the reaction
-
-
r
2 oxidized ferredoxin + NADPH + H+
2 reduced ferredoxin + NADP+
-
-
-
?
2 oxidized ferredoxin + NADPH + H+
2 reduced ferredoxin + NADP+
source of ferredoxin: Pisum sativum
-
-
?
2 oxidized ferredoxin + NADPH + H+
2 reduced ferredoxin + NADP+
source of ferredoxin: Pisum sativum
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
two transient charge-transfer complexes occur prior and upon hydride transfer in the reversible reaction, spectral properties and activities of wild-type and mutant enzymes, overview. Need for an adequate initial interaction between the 2'P-AMP portion of NADP+/H and FNR that provides subsequent conformational changes leading to charge-transfer complex formation
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
with K3[Fe(CN)6] as electron acceptor in the enzyme assay. Ferredoxin is a low-redox-potential iron-sulfur protein. BsFNR features two distinct binding domains for FAD and NADPH, the deduced mode of NADP+ binding to the BsFNR molecule is nonproductive in that the nicotinamide and isoalloxazine rings are over 15A A apart, binding structures, overview
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
cyt c-coupled assay, electron transfer system, overview
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
cyt c-coupled assay, electron transfer system, overview
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
source of ferredoxin: Leptospira LB107
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
source of ferredoxin: Leptospira LB107
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
the enzyme plays an important role in the redox cycle of ferredoxin in the archaeon
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
high specificity for NADPH, the activity with NADH is hardly observed without the addition of an external flavin
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
the enzyme plays an important role in the redox cycle of ferredoxin in the archaeon
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
high specificity for NADPH, the activity with NADH is hardly observed without the addition of an external flavin
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
ferredoxin Xac1762 is a potential substrate
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2,3-dichloro-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.035 V
-
-
?
2,3-dichloro-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.035 V
-
-
?
2,3-diglutathionyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.15 V
-
-
?
2,3-diglutathionyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
-
single electron reduction potential -0.15 V
-
-
?
2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
-
r
2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
-
r
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NADPH + H+
? + NADP+
-
-
-
?
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NADPH + H+
? + NADP+
-
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
-
diaphorase activity
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
-
FNR has also diaphorase activity
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
FNR has also diaphorase activity
-
-
?
methyl viologen + NADPH
reduced methyl viologen + NADP+
diaphorase activity
-
-
?
methyl viologen + NADPH
reduced methyl viologen + NADP+
diaphorase activity
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
diaphorase activity, cofactor specificity, overview
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
high diaphorase activity
-
-
?
NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[ferredoxin]
-
-
-
?
NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[ferredoxin]
-
-
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADH + FAD
NAD+ + reduced FAD
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADH
-
-
?
NADH + FAD
NAD+ + reduced FAD
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADH
-
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
diaphorase activity, acceptors can be complexed metals or aromatic molecules
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
diaphorase activity, acceptors can be complexed metals or aromatic molecules
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
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
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
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 several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, 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, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
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 several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
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
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
r
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
diaphorase activity, no activity with NADH
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
diaphorase activity
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
-
-
-
r
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
diaphorase reaction
-
-
ir
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
diaphorase reaction
-
-
ir
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
diaphorase activity
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
diaphorase activity
-
-
?
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
first enzyme in mitochondrial P-450-linked monooxygenase system catalyzing several steps in the biosynthesis of steroid hormones, bile acids or vitamin D3 in various tissues
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
key enzyme catalyzing the electron transport between NADPH generated by pentose phosphate pathway and ferredoxin in plastids of plant heterotrophic tissues
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
supports in vivo reduction of membrane bound adrenal mitochondrial P-450
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
ferredoxin is the preferred electron acceptor
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
Hydrogenobacter thermophilus expresses three ferredoxins: [4Fe-4S]-type Fd1 and Fd2, and [2Fe-2S]-type Fd3
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Hydrogenobacter thermophilus expresses three ferredoxins: [4Fe-4S]-type Fd1 and Fd2, and [2Fe-2S]-type Fd3
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
Chlorobaculum tepidum ATCC 49652
-
-
-
r
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
-
-
-
-
?
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
-
-
-
-
?
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
-
-
-
?
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
-
-
-
?
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
oxidized ferredoxin + NADPH + H+
reduced ferredoxin + NADP+
-
-
-
r
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
-
-
-
-
?
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
-
-
-
-
?
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
-
-
-
?
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
-
-
-
r
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
oxidized 2,6-dichlorophenolindophenol + NADPH
-
-
-
-
r
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
oxidized 2,6-dichlorophenolindophenol + NADPH
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
oxidized 2,6-dichlorophenolindophenol + NADPH
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+ + H+
oxidized 2,6-dichlorophenolindophenol + NADPH
-
-
-
-
r
reduced benzyl viologen + NADP+ + H+
oxidized benzyl viologen + NADPH
-
-
-
?
reduced benzyl viologen + NADP+ + H+
oxidized benzyl viologen + NADPH
-
-
-
?
reduced ferredoxin + NAD(P)+
oxidized ferredoxin + NAD(P)H
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
hydride transfer between FAD and NADP+, highly specific for NADP+ versus NAD+, mechnanism
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
hydride transfer of the N5 of the FAD isoalloxazine ring to the NADP+ nicotinamide ring, transfer of 2 electrons via the one-electron-carrier ferredoxin
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
plant-type ferredoxin contains a [2Fe2S] cluster, substrate is an acidic, bulky protein, enzyme-substrate interactions involve residues R16, K72, K75, R100, E139, R264, K290, and K294
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
substrate is a bulky protein
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
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
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
ferredoxin-dependent cytochrome c reduction, ferredoxin binding is independent of enzyme methylation status, positively charged residues K83 and K89 are required for activity
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
recombinant ferredoxin I and II, and ferredoxin I mutants, the Fd I Q39R/S28E mutant lacks the Arg39-Glu28 residues being essential for efficient electron transfer between the cofactor and the enzyme
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
substrate is a bulky protein
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reaction is performed in presence of CoA
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
reaction is performed in presence of CoA
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
low activity
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
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
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
NADPH is the reducing agent of FPR in vivo
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
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
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
terminal step in the non-cyclic photosynthetic electron transfer chain
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
ferredoxin contains a [2Fe2S] cluster and binds to the concave surface of the FAD domain, association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
plant-type ferredoxin contains a [2Fe2S] cluster, enzyme requires ferredoxin, substrate is a bulky protein, enzyme-substrate interactions involve residues R16, K72, K88, K116, E139, R264, K290, and K294, overview
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
generation of NADPH
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
enzyme is involved in the electron transfer cascade from photosystem I to NADP+, formation of a ternary complex between photosystem I, ferredoxin, and enzyme
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
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
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
structure of the ferredoxin-enzyme complex, ferredoxin binds to the concave region of the FAD domain, overview, release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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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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r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
Chlorobaculum tepidum ATCC 49652
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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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?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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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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?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
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r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
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r
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
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[4Fe-4S]-ferredoxin of Pseudomonas putida is similar to ferredoxin FdI of Azotobacter vinelandii, the Pseudomonas putida chromosome contains two [2Fe-2S] ferredoxins (FdA and FdB), three [4Fe-4S] ferredoxins (4FdA, 4FdB and FdxA) and one flavodoxin (Fld)
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r
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
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[4Fe-4S]-ferredoxin of Pseudomonas putida is similar to ferredoxin FdI of Azotobacter vinelandii, the Pseudomonas putida chromosome contains two [2Fe-2S] ferredoxins (FdA and FdB), three [4Fe-4S] ferredoxins (4FdA, 4FdB and FdxA) and one flavodoxin (Fld)
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r
additional information
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enzyme has also little NADP-2,6-dichlorophenol indophenol diaphorase activity
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additional information
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enzyme has also ferredoxin dependent cytochrome c reductase activity
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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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phylogenetic evolution, relationships, and classification, overview
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additional information
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coenzyme binding causes structural rearrangements of the protein backbone
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additional information
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NADPH-dependent cytochrome c reductase assay for determination of activity with ferredoxin or flavodoxin as electron carrier
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?
additional information
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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 highly irreversible
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?
additional information
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the enzyme is asscoiated to phycobilin pigments
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additional information
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phylogenetic evolution, relationships, and classification, overview
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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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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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?
additional information
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enzyme has also little NADP-2,6-dichlorophenol indophenol diaphorase activity
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?
additional information
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enzyme has also NADPH-NAD transhydrogenase 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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enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview
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?
additional information
?
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the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible
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?
additional information
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the enzyme also shows NAD(P)H oxidase activity, overview
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additional information
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH
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additional information
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH
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additional information
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH
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additional information
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phylogenetic evolution, relatiionships, and classification, overview
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?
additional information
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH, but not with NADH
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additional information
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH, but not with NADH
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additional information
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enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH, but not with NADH
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additional information
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phylogenetic evolution, relationships, and classification, overview
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additional information
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enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
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additional information
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specificity for tightly bound electron acceptors, overview
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additional information
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specificity for tightly bound electron acceptors, overview
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additional information
?
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the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible
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?
additional information
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the enzyme reduces flavodoxin I and flavodoxin II, reaction of EC 1.19.1.1, and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Ferredoxin binds to FNR with high affinity (Kd below 0.5 microM) and is reduced under single-turnover conditions. Flavodoxin I and flavodoxin II show affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin
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additional information
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the enzyme reduces flavodoxin I and flavodoxin II, reaction of EC 1.19.1.1, and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Ferredoxin binds to FNR with high affinity (Kd below 0.5 microM) and is reduced under single-turnover conditions. Flavodoxin I and flavodoxin II show affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin
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additional information
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enzyme has also ferredoxin dependent cytochrome c reductase activity
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additional information
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enzyme has also indonitrotetrazolium-violet diaphorase activity
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additional information
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enzyme has also NADPH-NAD transhydrogenase activity
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additional information
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phylogenetic evolution, relatiionships, and classification, overview
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additional information
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enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase
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additional information
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enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase
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additional information
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heme-iron scavenging by heme oxygenase in Leptospira. interrogans requires only plastidic-type ferredoxin-NADP+ reductase as redox partner. The enzyme provides the electrons for heme turnover by heme oxygenase
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additional information
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enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase
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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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no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein (reaction of EC 1.19.1.1). The observed rate constants for reoxidation of ferredoxin by FNR are about 100fold decreased when phenylglyoxal-modified FNR is used
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additional information
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no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein (reaction of EC 1.19.1.1). The observed rate constants for reoxidation of ferredoxin by FNR are about 100fold decreased when phenylglyoxal-modified FNR is used
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additional information
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enzyme has also irreversible NADPH-NAD+ transhydrogenase activity
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additional information
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enzyme has also low diaphorase activity
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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-cytochrome c reductase activity
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additional information
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FPR supports the efficient degradation of heme by heme oxygenase
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additional information
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shows negligible activity when NADP+ is replaced with NAD+
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additional information
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Fpr also catalyzes irreversible electron transfer (diaphorase activity), which drives the oxidation of NADPH in a wide variety of electron acceptors, such as viologens, quinines, complexed transition metals, and tetrazolium salts
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?
additional information
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Fpr also catalyzes irreversible electron transfer (diaphorase activity), which drives the oxidation of NADPH in a wide variety of electron acceptors, such as viologens, quinines, complexed transition metals, and tetrazolium salts
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additional information
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the enzyme does not perform NADH-dependent benzyl viologen reduction
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additional information
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the enzyme does not perform NADH-dependent benzyl viologen reduction
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additional information
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the enzyme does not perform NADH-dependent benzyl viologen reduction
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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-cytochrome c reductase activity
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additional information
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enzyme is involved in the antioxidant response and facilitation of the provision of reduced flavodoxin for the reduction of nitrogenase
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additional information
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phylogenetic evolution, relatiionships, and classification, overview
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?
additional information
?
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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 highly irreversible
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?
additional information
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after cross-linking ferredoxin to ferredoxin NADP+-reductase the enzyme maintains most of the diaphorase activity and gains capacity to catalyze the NADPH-cytochrome c reaction without addition of free ferredoxin
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additional information
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enzyme contains no FAD but shows NADP-specific diaphorase activity
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additional information
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truncated enzyme has no capacity to catalyze the ferredoxin-dependent reaction
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additional information
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enzyme has also NADPH-NAD transhydrogenase 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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enzyme has also NADPH-diaphorase 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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pathway of cyclic electron transport includes both ferredoxin and ferredoxin-NADP+ reductase, but not the NADP+-binding site of the reductase
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additional information
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ferredoxin-NADP+ reductase not involved in cyclic electron transport
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additional information
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enzyme is involved in cyclic electron transport and chlororespiration
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additional information
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enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview
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additional information
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structure-function analysis of isozymes and chimeric mutant thereof
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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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in vitro, the enzyme catalyses the NADPH-dependent reduction of various substrates, including ferredoxin, the analogue of its redox centre-ferricyanide, and the analogue of quinones, which is dibromothymoquinone
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?
additional information
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enzyme associated with the cytochrome b6f complex can participate in the cyclic electron transport in the chloroplast as photosystem I-plastoquinone or NADPH-plastoquinone oxidoreductase. Ferredoxin is not directly required for plastoquinone reduction but is rather necessary for the reduction of ferredoxin reductase under light conditions during operation of the cyclic electron transport
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?
additional information
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enzyme associated with the cytochrome b6f complex can participate in the cyclic electron transport in the chloroplast as photosystem I-plastoquinone or NADPH-plastoquinone oxidoreductase. Ferredoxin is not directly required for plastoquinone reduction but is rather necessary for the reduction of ferredoxin reductase under light conditions during operation of the cyclic electron transport
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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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the enzyme binds to phycocyanin hexamers
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additional information
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DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme. The enzyme is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin
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additional information
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DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme. The enzyme is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin
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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. NADH-dependent NADP+ reduction with reduced ferredoxin with a regenerating system composed of Fdox, ferredoxin-dependent [FeFe]-hydrogenase, and 100% H2 as a gas phase. The apparent Km value of NADPH is lower than that of NADH, and that of NADP+ is lower than that of NAD+. Notably, the NADP+-dependent reduction of NAD+ with Fdred is not feasible
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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
?
-
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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in vitro, the enzyme catalyses the NADPH-dependent reduction of various substrates, including ferredoxin, the analogue of its redox centre-ferricyanide, and the analogue of quinones, which is dibromothymoquinone
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?
additional information
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no substrates: pea ferredoxin, Escherichia coli ferredoxin, flavodoxin
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?
additional information
?
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no substrates: pea ferredoxin, Escherichia coli ferredoxin, flavodoxin
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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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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
?
-
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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?
