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+ NADPH + H+
? + NADP+
-
-
-
?
1,4-benzoquinone + NADP+
? + NADPH + H+
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+
-
-
-
?
1,4-naphthoquinone + NADP+
? + NADPH + H+
1,8-dihydroxy-9,10-anthraquinone + NADP+
? + NADPH + H+
1-oxo-1lambda5,2,4-benzotriazine + NADPH + H+
? + NADP+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
2 ferrocytochrome c + NAD+ + H+
2 ferricytochrome c + NADH
2 oxidized Fdx2 + NADPH + H+
2 reduced Fdx2 + NADP+
Fdx2 i.e. Chlamydomonas reinhardtii plant-type isoform ferredoxin 2
-
-
?
2 oxidized ferredoxin + NADH + H+
2 reduced ferredoxin + NAD+
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
2 oxidized ferredoxin + NADPH + H+
2 reduced ferredoxin + NADP+
2 reduced ferredoxin + NAD+
2 oxidized ferredoxin + NADH + H+
NAD+ is a poor substrate
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
2 reduced ferricyanide + NADP+
2 oxidized ferricyanide + NADPH
2,3-dichloro-1,4-naphthoquinone + NADP+
? + NADPH + H+
2,3-diglutathionyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
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+
-
-
-
?
2,6-dichlorophenolindophenol + NADPH + H+
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-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NADPH + H+
? + NADP+
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
-
-
?
cytochrome c + NADPH + H+
?
weakest substrate
-
-
?
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
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
FAD + NADPH + H+
reduced FAD + NADP+
-
-
-
?
Fe(III) citrate + NADH
Fe(II) citrate + NAD+
Fe(III) citrate + NADPH
Fe(II) citrate + NADP+
Fe(III)-deferoxamine + NADPH + H+
?
-
-
-
?
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)-EDTA + NADH
reduced Fe(III)-EDTA + NAD+
Fe(III)-EDTA + NADPH
reduced Fe(III)-EDTA + NADP+
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
Fe(III)-ferrichrome + NADPH + H+
?
-
-
-
?
Fe(III)-nitrilotriacetic acid + NADPH + H+
Fe(II) + nitrilotriacetic acid + NADP+
-
-
-
?
ferric citrate + NADPH + H+
?
-
-
-
?
ferric enterobactin + NADPH + H+
?
lowest activity
-
-
?
ferricyanide + NADP+
? + NADPH + H+
-
single electron acceptor, single electron reduction potential 0.41 V
-
-
?
ferricyanide + NADPH
ferrocyanide + NADP+ + H+
ferricytochrome c + NADP+
ferrocytochrome c + NADPH + H+
-
-
-
-
r
ferrocytochrome c + NADP+
ferricytochrome c + NADPH + H+
-
-
-
-
r
Fe[EDTA]- + NADP+
? + NADPH + H+
-
single electron acceptor, single electron reduction potential 0.12 V
-
-
?
FMN + NADPH + H+
reduced FMN + NADP+
-
-
-
?
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
?
K3Fe(CN)6 + NAD(P)H
?
-
-
-
?
K3Fe(CN)6 + NADPH
? + NADP+
-
-
-
-
?
menogarol + NADP+
7-deoxynogarol + NADPH
-
under anaerobic conditions
-
-
?
methyl (1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)carbamate + NADPH + H+
? + NADP+
-
-
-
?
methyl viologen + NADPH
reduced methyl viologen + 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
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 + FAD
NAD+ + reduced FAD
NADH + K3Fe(CN)6
NAD+ + reduced K3Fe(CN)6
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
NADPH + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride
NADP+ + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride
-
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
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 + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
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
NAD+ + reduced 2,6-dichlorophenolindophenol
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+
?
-
-
-
?
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 + NADH + H+
reduced ferredoxin + NAD+
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
oxidized ferredoxin + NADPH + H+
reduced ferredoxin + NADP+
oxidized ferredoxin I + NADH + H+
reduced ferredoxin I + NAD+
-
-
-
-
?
oxidized ferredoxin I + NADPH + H+
reduced ferredoxin I + NADP+
-
-
-
-
r
oxidized ferredoxin II + NADPH + H+
reduced ferredoxin II NADP+
-
-
-
-
r
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
-
-
?
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
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 benzyl viologen + NADP+ + H+
oxidized benzyl viologen + NADPH
reduced cytochrome c + NADP+
oxidized cytochrome c + NADPH + H+
-
-
-
?
reduced ferredoxin + NAD(P)+
oxidized ferredoxin + NAD(P)H
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH
-
the rate of NADH oxidation by FNR is lower than that with NADPH
-
-
r
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
reduced ferredoxin I + NADP+
oxidized ferredoxin I + NADPH
-
-
-
-
r
reduced ferredoxin I + NADP+
oxidized ferredoxin I + NADPH + H+
reduced ferredoxin II + NADP+
oxidized ferredoxin II + NADPH + H+
-
-
-
-
r
reduced ferricyanide + NADP+ + H+
ferrocyanide + NADPH
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
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+
-
-
-
?
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
additional information
?
-
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+
-
diaphorase reaction
-
-
ir
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+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
diaphorase reaction
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
i.e. K3Fe(CN)6, diaphorase activity
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
?
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+
-
-
-
-
r
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+
-
-
-
-
r
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+
-
-
-
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+
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2 reduced ferricyanide + NADP+
2 oxidized ferricyanide + NADPH
-
-
-
-
r
2 reduced ferricyanide + NADP+
2 oxidized ferricyanide + NADPH
-
-
-
-
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
-
-
?
Fe(III) citrate + NADH
Fe(II) citrate + NAD+
-
-
-
-
?
Fe(III) citrate + NADH
Fe(II) citrate + NAD+
-
-
-
-
?
Fe(III) citrate + NADPH
Fe(II) citrate + NADP+
-
-
-
-
?
Fe(III) citrate + NADPH
Fe(II) citrate + NADP+
-
-
-
-
?
Fe(III)-EDTA + NADH
reduced Fe(III)-EDTA + NAD+
-
-
-
-
?
Fe(III)-EDTA + NADH
reduced Fe(III)-EDTA + NAD+
-
-
-
-
?
Fe(III)-EDTA + NADPH
reduced Fe(III)-EDTA + NADP+
-
-
-
-
?
Fe(III)-EDTA + NADPH
reduced Fe(III)-EDTA + NADP+
-
-
-
-
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
-
-
-
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
-
-
-
?
ferricyanide + NADPH
ferrocyanide + NADP+ + H+
-
-
-
-
r
ferricyanide + NADPH
ferrocyanide + NADP+ + H+
-
-
-
-
r
ferricyanide + NADPH
ferrocyanide + NADP+ + H+
-
-
-
-
r
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
-
-
?
NADH + K3Fe(CN)6
NAD+ + reduced K3Fe(CN)6
-
-
-
-
r
NADH + K3Fe(CN)6
NAD+ + reduced K3Fe(CN)6
-
-
-
-
r
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
-
-
-
-
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
-
-
-
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 + 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
-
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
?
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
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
supports in vivo reduction of membrane bound adrenal mitochondrial P-450
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
-
-
-
?
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+
-
-
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
-
-
r
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+
-
-
-
-
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+
-
-
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
-
-
-
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
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 + NAD(P)+
oxidized ferredoxin + NAD(P)H
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
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
-
-
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
-
-
-
-
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
-
-
-
-
?, 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
-
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
-
-
-
-
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
-
-
-
-
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
-
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
-
-
-
-
r
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
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reaction is performed in presence of CoA
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
reaction is performed in presence of CoA
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
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
-
low activity
-
-
?
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
-
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
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
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
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
generation of NADPH
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
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
-
-
-
-
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
-
-
-
-
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+
oxidized ferredoxin + NADPH + H+
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?, r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin I + NADP+
oxidized ferredoxin I + NADPH + H+
-
-
-
-
r
reduced ferredoxin I + NADP+
oxidized ferredoxin I + NADPH + H+
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
r
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
-
[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)
-
-
r
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
-
[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)
-
-
r
additional information
?
-
-
enzyme has also little NADP-2,6-dichlorophenol indophenol diaphorase activity
-
-
?
additional information
?
-
-
enzyme has also ferredoxin dependent cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
coenzyme binding causes structural rearrangements of the protein backbone
-
-
?
additional information
?
-
-
NADPH-dependent cytochrome c reductase assay for determination of activity with ferredoxin or flavodoxin as electron carrier
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is asscoiated to phycobilin pigments
-
-
?
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
the enzyme does not interact with Arabidopsis ferredoxin 1
-
-
?
additional information
?
-
-
enzyme has also little NADP-2,6-dichlorophenol indophenol diaphorase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-NAD transhydrogenase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
?
additional information
?
-
-
involved in oxidative stress
-
-
?
additional information
?
-
-
enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme also shows NAD(P)H oxidase activity, overview
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
specificity for tightly bound electron acceptors, overview
-
-
?
additional information
?
-
specificity for tightly bound electron acceptors, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
enzyme has also ferredoxin dependent cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme has also indonitrotetrazolium-violet diaphorase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-NAD transhydrogenase activity
-
-
?
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase
-
-
?
additional information
?
-
-
enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
enzyme has also irreversible NADPH-NAD+ transhydrogenase activity
-
-
?
additional information
?
-
-
enzyme has also low diaphorase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
?
additional information
?
-
-
FPR supports the efficient degradation of heme by heme oxygenase
-
-
?
additional information
?
-
-
shows negligible activity when NADP+ is replaced with NAD+
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme does not perform NADH-dependent benzyl viologen reduction
-
-
?
additional information
?
-
-
the enzyme does not perform NADH-dependent benzyl viologen reduction
-
-
?
additional information
?
-
the enzyme does not perform NADH-dependent benzyl viologen reduction
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme is involved in the antioxidant response and facilitation of the provision of reduced flavodoxin for the reduction of nitrogenase
-
-
?
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme contains no FAD but shows NADP-specific diaphorase activity
-
-
?
additional information
?
-
-
truncated enzyme has no capacity to catalyze the ferredoxin-dependent reaction
-
-
?
additional information
?
-
-
enzyme has also NADPH-NAD transhydrogenase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
?
additional information
?
-
enzyme has also NADPH-diaphorase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
?
additional information
?
-
-
pathway of cyclic electron transport includes both ferredoxin and ferredoxin-NADP+ reductase, but not the NADP+-binding site of the reductase
-
-
?
additional information
?
-
-
ferredoxin-NADP+ reductase not involved in cyclic electron transport
-
-
?
additional information
?
-
-
enzyme is involved in cyclic electron transport and chlororespiration
-
-
?
additional information
?
-
-
enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
-
structure-function analysis of isozymes and chimeric mutant thereof
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
the enzyme binds to phycocyanin hexamers
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no substrates: pea ferredoxin, Escherichia coli ferredoxin, flavodoxin
-
-
?
additional information
?
-
-
no substrates: pea ferredoxin, Escherichia coli ferredoxin, flavodoxin
-
-
?
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
?
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
-
the enzyme also shows NADPH-dependent cyt c reductase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 oxidized ferredoxin + NADPH
2 reduced ferredoxin + NADP+ + H+
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH + H+
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
additional information
?
-
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 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+
-
-
-
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+
-
-
-
-
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+
-
-
-
-
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+
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+
-
-
-
-
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+
-
-
-
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+
-
-
-
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 ferredoxin + NADPH
reduced ferredoxin + NADP+
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
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 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+
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+ + H+
-
-
-
r
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
-
-
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
-
-
-
-
?
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
-
-
-
-
r
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
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
-
r
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
-
-
-
-
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
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
-
-
-
?
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
-
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
-
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+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?, r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
-
-
-
?
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
-
[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)
-
-
r
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
-
[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)
-
-
r
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
-
involved in oxidative stress
-
-
?
additional information
?
-
-
enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
-
enzyme is involved in the antioxidant response and facilitation of the provision of reduced flavodoxin for the reduction of nitrogenase
-
-
?
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
-
pathway of cyclic electron transport includes both ferredoxin and ferredoxin-NADP+ reductase, but not the NADP+-binding site of the reductase
-
-
?
additional information
?
-
-
ferredoxin-NADP+ reductase not involved in cyclic electron transport
-
-
?
additional information
?
-
-
enzyme is involved in cyclic electron transport and chlororespiration
-
-
?
additional information
?
-
-
enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
?
additional information
?
-
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.095
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride
at 25°C in 200 mM Tris-HCl (pH 9.0), containing 70 mM NaCl and 0.1% Triton-X100
0.0119 - 0.0132
dibromothymoquinone
0.00364 - 0.0396
Fe(III)-EDTA
0.012 - 0.053
Ferredoxin
-
0.29
ferricyanide
-
at pH 7.0 and 25°C
0.00205 - 0.01103
ferricytochrome c
0.03 - 0.0547
iodonitrotetrazolium violet
-
4 different fractions after ferredoxin-Sepharose chromatography
0.097 - 0.1
K3Fe(CN)6
-
-
0.036 - 0.083
oxidized 2,6-dichlorophenolindophenol
0.0066
oxidized Fdx2
pH 7.5, 25°C
-
0.00027 - 0.54
oxidized ferredoxin
0.0114
oxidized ferredoxin I
-
wild-type cofactor, pH 7.5, 25°C
-
0.0017
oxidized ferredoxin II
-
wild-type cofactor, pH 7.5, 25°C
-
0.0053
oxidized ferredoxin II mutant D64N
-
pH 7.5, 25°C
-
0.0115
oxidized ferredoxin II mutant Q39R/S28E
-
pH 7.5, 25°C
-
0.0195 - 0.032
oxidized [2Fe-2S]-[rubredoxin]
-
0.46
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
at pH 7.5 and 22°C
-
0.01 - 0.058
reduced 2,6-dichlorophenolindophenol
0.0012 - 0.051
reduced ferredoxin
0.0025 - 0.0027
reduced ferredoxin I
-
0.0074
reduced ferricyanide
-
at pH 8.7 and 22°C
additional information
additional information
-
0.0119
dibromothymoquinone
-
-
0.0132
dibromothymoquinone
-
in presence of Cd2+
0.015
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25°C, with NADH
0.022
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
0.00364
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.0396
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.012
Ferredoxin
pH 8.0, 25°C
-
0.049
Ferredoxin
-
35 kDa enzyme
-
0.053
Ferredoxin
-
32 kDa enzyme
-
0.00205
ferricytochrome c
-
mutant bearing a lysine to glutamine mutation in the first lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication
0.00312
ferricytochrome c
-
wild-type, pH 7.5, temperature not specified in the publication
0.0035
ferricytochrome c
-
mutant bearing a lysine to glutamine mutation in the second lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication
0.00999
ferricytochrome c
-
mutant bearing an N-terminal region with the full wheat KISKK domain, pH 7.5, temperature not specified in the publication
0.0103
ferricytochrome c
-
mutant bearing a truncated N-terminal domain beginning after the KISKK domain, pH 7.5, temperature not specified in the publication
0.0104
ferricytochrome c
-
mutant bearing lysine to glutamine mutations in the second and third lysine residues of the KISKK domain, pH 7.5, temperature not specified in the publication
0.01103
ferricytochrome c
-
mutant with an extended N-terminal region to include the EAxxPA motif of maize, pH 7.5, temperature not specified in the publication
0.00112
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.00235
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00273
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00298
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.003
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.00338
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.0037
NADH
mutant lacking the beta-hairpin, pH 8.0, 30°C
0.00464
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0059
NADH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
0.00616
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0065
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.0065
NADH
mutant DELTAW248, pH 8.0, 30°C
0.007
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.00717
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.00802
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.00822
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00866
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.00933
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.00943
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.01063
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.01163
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.01238
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0129
NADH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.0143
NADH
wild-type, pH 8.0, 30°C
0.01866
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.02363
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.0394
NADH
mutant T155G/A160T/L263P/Y303S, called PP3CT
0.05625
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.0632
NADH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.064
NADH
mutant T155G/A160T/L263P/R264P/G265P, called PP5
0.1076
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.18
NADH
mutant T155G, pH 8.0
0.39
NADH
mutant T155G/A160T/L263P, pH 8.0
0.39
NADH
mutant T155G/A160T/L263P, called PP3
0.51
NADH
mutant T155G/A160T, pH 8.0
0.63
NADH
mutant L263A, pH 8.0
0.65
NADH
mutant L263P, pH 8.0
0.72
NADH
with K3Fe(CN)6 as cosubstrate, at 25°C, in 100 mM Tris-HCl (pH 8.2)
0.8
NADH
wild-type enzyme, pH 8.0
0.8
NADH
wild type enzyme of Anabaena sp.
1.25
NADH
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
1.323
NADH
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
1.5
NADH
mutant S223D/R233L/Y235F, pH 8.0
2.3
NADH
mutant R233L/Y235F, pH 8.0
3
NADH
mutant T155G/R224Q/R233L/Y235F, pH 8.0
3.3
NADH
pH 8.0, temperature not specified in the publication
4.2
NADH
-
pH 7.0, 15°C, recombinant chimeric enzyme
4.3
NADH
mutant R224Q/R233L/Y235F, pH 8.0
12
NADH
mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
0.00722
NADP+
-
-
0.00045
NADPH
-
recombinant enzyme, pH 8.2, 25°C, with Fe(CN)63-
0.00083
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00089
NADPH
-
recombinant enzyme, pH 8.2, 25°C, with 2,6-dichlorophenolindophenol
0.0011
NADPH
-
in a quinone-dependent cytochrome c reduction assay
0.0011
NADPH
in a quinone-dependent cytochrome c reduction assay
0.00111
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.0012
NADPH
-
wild-type, 30°C, pH 8.0
0.0016
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
0.0018
NADPH
in the presence of 0.15 mM Fe(III)-EDTA, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.00181
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.0019
NADPH
pH 7.0, 25°C, recombinant mutant Y50S
0.00191
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.00191
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.0024
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0
0.0024
NADPH
mutant DELTAW248, pH 8.0, 30°C
0.00245
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0026
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0
0.00263
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.003
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.0031
NADPH
-
in presence of Cd2+
0.00326
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0034
NADPH
-
recombinant mutant E139Q, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.0036
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
0.0037
NADPH
-
pH 7.4, temperature not specified in the publication, recombinant enzyme
0.00397
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.004
NADPH
-
in a ferredoxin-dependent cytochrome c reduction assay
0.004
NADPH
in a ferredoxin-dependent cytochrome c reduction assay
0.004
NADPH
pH 7.0, 25°C, recombinant mutant Y50W
0.0041
NADPH
mutant T155G/A160T/L263P/Y303S, called PP3CT
0.0043
NADPH
pH 7.0, 25°C, recombinant mutant Y50G
0.00457
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.00459
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.0047
NADPH
-
recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.00479
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.0055
NADPH
using cytochrome c as electron acceptor
0.0058
NADPH
-
recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.00587
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.006
NADPH
wild-type enzyme, pH 8.0
0.006
NADPH
-
recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.006
NADPH
wild type enzyme of Anabaena sp.
0.00615
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.00625
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00636
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0066
NADPH
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
0.00666
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.00686
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.007
NADPH
-
native enzyme, pH 8.0, 30°C
0.0074
NADPH
-
pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity
0.00751
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.0083
NADPH
wild-type, pH 8.0, 30°C
0.009
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.0094
NADPH
-
pH 8.2, temperature not specified in the publication, recombinant enzyme
0.01
NADPH
-
INT as electron acceptor
0.01
NADPH
using K3Fe(CN)6 as electron acceptor
0.0108
NADPH
pH 8.0, temperature not specified in the publication
0.011
NADPH
-
in a 2,6-dichlorophenolindophenol reduction assay
0.011 - 0.035
NADPH
-
ferredoxin-dependent cytochrome c reductase activity
0.01177
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.012
NADPH
-
K3Fe(CN)6 as electron acceptor
0.012
NADPH
mutant T155G/A160T/L263P, pH 8.0
0.012
NADPH
-
pH 7.0, 15°C, wild-type root isozyme, diaphorase activity
0.012
NADPH
mutant T155G/A160T/L263P, called PP3
0.0125
NADPH
-
enzyme in PBS, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
0.01319
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.0142
NADPH
-
with 2 mM ferricyanide in 20 mM HEPES-NaOH buffer, at pH 7.0 and 25°C
0.01424
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.0147
NADPH
mutant lacking the beta-hairpin, pH 8.0, 30°C
0.015
NADPH
mutant L263A, pH 8.0
0.015
NADPH
-
wild-type, pH 9.0, 25°C
0.0153
NADPH
wild-type, pH 8.0, 30°C
0.01544
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.016
NADPH
-
mutant lacking amino acids 81 to 118, pH 9.0, 25°C
0.0163
NADPH
-
enzyme in soluble extract, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
0.019
NADPH
mutant L263P, pH 8.0
0.0195
NADPH
in 50 mM Tris-HCl, pH 8, at 30°C
0.0197
NADPH
pH 7.0, 25°C, recombinant wild-type enzyme
0.02
NADPH
in a 2,6-dichlorophenolindophenol reduction assay
0.02
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.02
NADPH
-
with ferricyanide as cosubstrate, at pH 7.0 and 25°C
0.0207
NADPH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
0.022
NADPH
mutant T155G/A160T, pH 8.0
0.022
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
0.023
NADPH
mutant T155G, pH 8.0
0.023
NADPH
mutant T155G/A160T/L263P/R264P/G265P, called PP5
0.0242
NADPH
-
pH 6.8, temperature not specified in the publication, recombinant enzyme
0.02967
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.032
NADPH
mutant A266Y, substrate ferricyanide, pH 7.2, 25°C
0.033
NADPH
-
recombinant enzyme, pH 8.0, 30°C
0.033 - 0.062
NADPH
-
NADPH-2,6-dichlorophenol indophenol diaphorase activity
0.035
NADPH
-
pH 7.0, 15°C, wild-type leaf isozyme, diaphorase activity
0.035
NADPH
-
both wild-type and mutant Q242R
0.036
NADPH
with K3Fe(CN)6 as cosubstrate, at 25°C, in 100 mM Tris-HCl (pH 8.2)
0.036
NADPH
in an assay using K3Fe(CN)6 as electron acceptor
0.036 - 0.043
NADPH
-
multiple forms of ferredoxin-NADP+ reductase
0.039
NADPH
mutant A266Y/Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.05
NADPH
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
0.057
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
0.059
NADPH
-
diaphorase activity enzyme I
0.067
NADPH
-
diaphorase activity enzyme II
0.071
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
0.085
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.093
NADPH
wild-type, substrate ferricyanide, pH 7.2, 25°C
0.14
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
0.35
NADPH
cosubstrate 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride, 25°C, pH 9.0
0.35
NADPH
with 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride as cosubstrate, at 25°C, in 100 mM Tris-HCl (pH 8.2)
0.37
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
0.4
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
0.52
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
0.57
NADPH
-
2,6-dichlorophenolindophenol reduction, pH 7.0, 24°C
0.8
NADPH
diaphorase activity, pH 8.0
1.366
NADPH
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
1.7
NADPH
mutant R233L/Y235F, pH 8.0
1.8
NADPH
above, mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
2.7
NADPH
mutant T155G/R224Q/R233L/Y235F, pH 8.0
3.6
NADPH
mutant R224Q/R233L/Y235F, pH 8.0
0.036
oxidized 2,6-dichlorophenolindophenol
-
diaphorase activity enzyme I
0.047
oxidized 2,6-dichlorophenolindophenol
-
diaphorase activity enzyme II
0.068
oxidized 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with Fe(CN)63-
0.083
oxidized 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with 2,6-dichlorophenolindophenol
0.00027
oxidized ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM
0.0005
oxidized ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM
0.0008
oxidized ferredoxin
Plasmodium falciparum ferredoxin PfFd is tested;using cytochrome c as electron acceptor
0.0009
oxidized ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM
0.0009
oxidized ferredoxin
mutant lacking the beta-hairpin, pH 8.0, 30°C
0.0009
oxidized ferredoxin
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
0.0014
oxidized ferredoxin
wild-type, pH 8.0, 30°C
0.0018
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
0.0022
oxidized ferredoxin
wild-type, pH 8.0, 30°C
0.0025
oxidized ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 100 mM
0.0035
oxidized ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM
0.0043
oxidized ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM
0.0062
oxidized ferredoxin
mutant DELTAW248, pH 8.0, 30°C
0.0076
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.02
oxidized ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM
0.021
oxidized ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM
0.023
oxidized ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 100 mM
0.023
oxidized ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 28 mM
0.039
oxidized ferredoxin
pH 7.5, 25°C
0.1
oxidized ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM
0.4
oxidized ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 200 mM
0.54
oxidized ferredoxin
-
with NADPH, pH 7.0, 24°C
0.0195
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADH, pH 7, 25°C
-
0.021
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
0.032
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
0.01 - 0.016
reduced 2,6-dichlorophenolindophenol
-
NADPH-2,6-dichlorophenol-indophenol diaphorase activity
0.056
reduced 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADH
0.058
reduced 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
0.0012
reduced ferredoxin
-
-
0.0022
reduced ferredoxin
-
at pH 7.5 and 20°C
0.0022
reduced ferredoxin
-
at pH 7.5 and 25°C
0.0023
reduced ferredoxin
-
at pH 7.5 and 15°C
0.0024
reduced ferredoxin
-
at pH 7.5 and 30°C
0.0026
reduced ferredoxin
-
native enzyme, pH 8.0, 30°C
0.0028
reduced ferredoxin
-
mutant lacking amino acids 81 to 118, pH 8.2, 25°C
0.0038
reduced ferredoxin
-
enzyme II
0.0043
reduced ferredoxin
-
enzyme I
0.0045 - 0.0046
reduced ferredoxin
-
ferredoxin-dependent cytochrome c reductase activity
0.005
reduced ferredoxin
-
-
0.0058
reduced ferredoxin
-
pH 8.0, 13°C, mutant Y308F
0.0065
reduced ferredoxin
-
pH 8.0, 13°C, wild-type enzyme
0.0066
reduced ferredoxin
-
recombinant enzyme, pH 8.0, 30°C
0.009
reduced ferredoxin
-
pH 8.0, 13°C, mutant Y308S
0.011
reduced ferredoxin
pH 8.0, 13°C, wild-type enzyme
0.012
reduced ferredoxin
pH 8.0, 25°C
0.017
reduced ferredoxin
-
pH 8.0, 13°C, mutant Y308W
0.018
reduced ferredoxin
-
wild-type, pH 8.2, 25°C
0.051
reduced ferredoxin
pH 8.0, 13°C, mutant Y303F
0.0025
reduced ferredoxin I
-
pH 7.0, 15°C, wild-type root isozyme
-
0.0026
reduced ferredoxin I
-
pH 7.0, 15°C, wild-type leaf isozyme
-
0.0027
reduced ferredoxin I
-
pH 7.0, 15°C, recombinant chimeric enzyme
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
increasing NH4Cl concentration enhances Km
-
additional information
additional information
-
enzyme reacts slower with different mutants of ferredoxin than with wild type ferredoxin
-
additional information
additional information
-
Km value of different mutants
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
Km value increases with pH
-
additional information
additional information
-
enzyme covalently cross-linked to flavodoxin
-
additional information
additional information
-
increasing light intensity reduces Km
-
additional information
additional information
kinetics, wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
below 0.1 mM, oxidized ferredoxin with NADH, pH 7.0, 24°C
-
additional information
additional information
-
detailed binding kinetics, detailed reaction kinetics, enzyme-substrate complex formation
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
-
gradual decrease in activity according to biphasic kinetics within 120 min
-
additional information
additional information
-
kinetics, rapid thermal inactivation of reduced enzyme and drop of activity
-
additional information
additional information
-
steady-state kinetics and dissociation constants of NADPH-enzyme complex, wild-type isozymes and recombinant chimera
-
additional information
additional information
-
stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes
-
additional information
additional information
stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes
-
additional information
additional information
-
stopped-flow kinetics measurements, pH 8.0, 13°C, steady-state kinetics for wild-type and mutant enzymes dependent on ionic strength, overview
-
additional information
additional information
-
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
-
additional information
additional information
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
analysis of kinetic rate constants for the reaction of enzyme with NADP+/NADPH
-
additional information
additional information
-
Fpr showed high specificity for NADPH; Km value for NADPH is <5 microMol, whereas that for NADH is above 2 mM
-
additional information
additional information
-
stopped flow kinetic analysis
-
additional information
additional information
-
Stopped-flow pre-steady-state kinetics, overview
-
additional information
additional information
-
kinetic evidence for its bifurcating behavior of the enzyme, cofactor kinetics, overview
-
additional information
additional information
spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview
-
additional information
additional information
-
spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
21 - 37
2,6-dichlorophenolindophenol
12.6 - 25
dibromothymoquinone
248
oxidized Fdx2
pH 7.5, 25°C
-
0.15 - 252
oxidized ferredoxin
16.5 - 255
oxidized [2Fe-2S]-[rubredoxin]
-
0.43
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
at pH 7.5 and 22°C
-
0.15 - 600
reduced ferredoxin
45 - 177
reduced ferredoxin I
-
32.2 - 147
reduced ferredoxin II
-
0.43
reduced ferricyanide
-
at pH 8.7 and 22°C
0.004 - 139.4
reduced flavodoxin
0.0042
reduced flavodoxin I
pH 8.0, 25°C
-
0.0039
reduced flavodoxin II
pH 8.0, 25°C
-
19
reduced flavodoxin mutant I59A
-
using cytochrome c as electron acceptor, for mutant I59A
-
15.3
reduced flavodoxin mutant I59A/I92A
-
using cytochrome c as electron acceptor, for mutant I59A/I92A
-
27.5
reduced flavodoxin mutant I59E
-
using cytochrome c as electron acceptor, for mutant I59E
-
14
reduced flavodoxin mutant I59E/I92E
-
using cytochrome c as electron acceptor, for mutant I59E/I92E
-
25.8
reduced flavodoxin mutant I92A
-
using cytochrome c as electron acceptor, for mutant I92A
-
26.5
reduced flavodoxin mutant I92E
-
using cytochrome c as electron acceptor, for mutant I92E
-
13.8
reduced flavodoxin mutant W57E
-
using cytochrome c as electron acceptor, for mutant W57E
-
90.3
reduced flavodoxin mutant W57K
-
using cytochrome c as electron acceptor, for mutant W57K
-
52.7
reduced flavodoxin mutant W57R
-
using cytochrome c as electron acceptor, for mutant W57R
-
additional information
additional information
-
21
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADH
25.6
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
35
2,6-dichlorophenolindophenol
-
native enzyme, pH 8.0, 30°C
37
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.0, 30°C
12.6
dibromothymoquinone
-
in presence of Cd2+
25
dibromothymoquinone
-
-
42
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25°C, with NADH
63
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
3
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C
3.53
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.0005
NADH
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
0.008
NADH
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
0.02
NADH
mutant T155G, pH 8.0
0.04
NADH
mutant S223D/R224Q/R233L/Y235F, pH 8.0
0.04
NADH
mutant T155G/A160T/S223D/R224Q/R233L/Y235F, pH 8.0
0.05
NADH
mutant L263P, pH 8.0
0.06
NADH
mutant T155G/S223D/R224Q/R233L/Y235F, pH 8.0
0.07
NADH
mutant T155G/A160T, pH 8.0
0.1
NADH
mutant S223D/R233L/Y235F, pH 8.0
0.13
NADH
mutant L263A, pH 8.0
0.16
NADH
wild-type enzyme, pH 8.0
0.16
NADH
wild type enzyme of Anabaena sp.
0.28
NADH
mutant T155G/R224Q/R233L/Y235F, pH 8.0
0.33
NADH
mutant T155G/A160T/L263P, pH 8.0
0.33
NADH
mutant T155G/A160T/L263P, called PP3
0.4
NADH
-
ferredoxin reduction, pH 7.0, 24°C
0.65
NADH
mutant T155G/A160T/L263P/R264P/G265P, called PP5
0.86
NADH
mutant R233L/Y235F, pH 8.0
1.16
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
1.2
NADH
mutant R224Q/R233L/Y235F, pH 8.0
2
NADH
mutant lacking the beta-hairpin, pH 8.0, 30°C
2.1
NADH
mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
3.03
NADH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
3.09
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
3.11
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
3.2
NADH
pH 8.0, temperature not specified in the publication
4.59
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
5
NADH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
5.6
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
7
NADH
wild-type, pH 8.0, 30°C
7.71
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
8.21
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
9.18
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
9.6
NADH
-
pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity
10
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
10.18
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
10.64
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
13.2
NADH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
16.44
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
17.47
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
19.24
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
31
NADH
mutant T155G/A160T/L263P/Y303S, called PP3CT
45.3
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
54.1
NADH
mutant DELTAW248, pH 8.0, 30°C
0.0003
NADPH
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
0.02
NADPH
mutant T155G/A160T/S223D/R224Q/R233L/Y235F, pH 8.0
0.03
NADPH
mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
0.05
NADPH
mutant S223D/R224Q/R233L/Y235F, pH 8.0
0.06
NADPH
mutant T155G/S223D/R224Q/R233L/Y235F, pH 8.0
0.2
NADPH
mutant T155G/R224Q/R233L/Y235F, pH 8.0
0.24
NADPH
-
pH 7.4, temperature not specified in the publication, recombinant enzyme
0.6
NADPH
-
pH 8.2, temperature not specified in the publication, recombinant enzyme
1
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
1.3
NADPH
mutant R224Q/R233L/Y235F, pH 8.0
1.91
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
2.2
NADPH
-
wild-type, 30°C, pH 8.0
3.2
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
3.7
NADPH
-
NADPH cytochrome c reductase activity, flavodoxin
3.8
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286K
3.82
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
4.51
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
4.77
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
5.99
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
6
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
6.18
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
6.8
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
7
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
7.13
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
7.2
NADPH
diaphorase activity, pH 8.0
7.5
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
7.5
NADPH
using cytochrome c as electron acceptor
7.54
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
8
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
10.1
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0
10.28
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
10.77
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
11.18
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
11.92
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
12
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
12.5
NADPH
-
in presence of Cd2+
16.2
NADPH
pH 7.0, 25°C, recombinant mutant Y50S
17
NADPH
mutant L263P, pH 8.0
17.5
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
20
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
20.38
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
21.71
NADPH
-
pH 6.8, temperature not specified in the publication, recombinant enzyme
21.72
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
22
NADPH
mutant R233L/Y235F, pH 8.0
22.6
NADPH
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
22.7
NADPH
-
2,6-dichlorophenolindophenol reduction, pH 7.0, 24°C
24.5
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
27
NADPH
-
electron transfer via the enzyme to Fe(CN)63-
35
NADPH
mutant T155G/A160T/L263P/R264P/G265P, called PP5
35.4
NADPH
-
ferredoxin reduction, pH 7.0, 24°C
37.61
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
38.2
NADPH
wild-type, pH 8.0, 30°C
38.5
NADPH
mutant T155G/A160T/L263P/Y303S, called PP3CT
42.8
NADPH
pH 7.0, 25°C, recombinant mutant Y50G
44.5
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
55
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
56.1
NADPH
-
enzyme in soluble extract, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
59
NADPH
-
recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
60
NADPH
mutant L263A, pH 8.0
65
NADPH
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
68
NADPH
mutant A266Y, substrate ferricyanide, pH 7.2, 25°C
70
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
72
NADPH
mutant T155G/A160T, pH 8.0
73.5
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0
74.1
NADPH
-
wild-type, 30°C, pH 8.0
77
NADPH
mutant T155G/A160T/L263P, pH 8.0
77
NADPH
mutant T155G/A160T/L263P, called PP3
81
NADPH
-
recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
81.5
NADPH
wild-type enzyme, pH 8.0
81.5
NADPH
wild type enzyme of Anabaena sp.
85
NADPH
using K3Fe(CN)6 as electron acceptor
86
NADPH
-
enzyme in PBS, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
88
NADPH
-
recombinant mutant E139Q, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
89
NADPH
-
recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
95.5
NADPH
mutant DELTAW248, pH 8.0, 30°C
97
NADPH
mutant T155G, pH 8.0
99
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
100
NADPH
-
NADPH cytochrome c reductase activity, ferredoxin
105
NADPH
-
NADPH-dichlorophenol indophenol diaphorase activity
121.9
NADPH
pH 8.0, temperature not specified in the publication
125
NADPH
in an assay using K3Fe(CN)6 as electron acceptor
183
NADPH
pH 7.0, 25°C, recombinant mutant Y50W
185
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
213
NADPH
-
with 2 mM ferricyanide in 20 mM HEPES-NaOH buffer, at pH 7.0 and 25°C
222
NADPH
wild-type, substrate ferricyanide, pH 7.2, 25°C
225
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
225 - 520
NADPH
-
electron transfer via the enzyme to K3Fe(CN)6
233
NADPH
-
NADPH-ferredoxin-cytochrome c reductase activity
250
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
251.1
NADPH
mutant lacking the beta-hairpin, pH 8.0, 30°C
258
NADPH
in 50 mM Tris-HCl, pH 8, at 30°C
267
NADPH
-
diaphorase activity, FNR-flavodoxin complex
360.5
NADPH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
374.3
NADPH
wild-type, pH 8.0, 30°C
424
NADPH
-
mutant lacking pH 9.0, 25°C
500
NADPH
-
pH 7.0, 15°C, wild-type leaf isozyme, diaphorase activity
517
NADPH
-
NADPH-ferricyanide diaphorase activity
517
NADPH
-
diaphorase activity
520
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
520
NADPH
-
pH 7.0, 15°C, wild-type root isozyme, diaphorase activity
540
NADPH
-
wild-type, pH 9.0, 25°C
550
NADPH
-
electron transfer via the enzyme to K3Fe(CN)6
560
NADPH
-
pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity
930
NADPH
-
with ferricyanide as cosubstrate, at pH 7.0 and 25°C
1012
NADPH
pH 7.0, 25°C, recombinant wild-type enzyme
0.15
oxidized ferredoxin
-
with NADPH
3.7
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
4.6
oxidized ferredoxin
mutant DELTAW248, pH 8.0, 30°C
19.4
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
22.8
oxidized ferredoxin
wild-type, pH 8.0, 30°C
32.7
oxidized ferredoxin
mutant lacking the beta-hairpin, pH 8.0, 30°C
35.9
oxidized ferredoxin
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
75
oxidized ferredoxin
wild-type, pH 8.0, 30°C
252
oxidized ferredoxin
pH 7.5, 25°C
16.5
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADH, pH 7, 25°C
-
24.8
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
255
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
0.15
reduced ferredoxin
-
-
0.15
reduced ferredoxin
pH 8.0, 25°C
1
reduced ferredoxin
pH 8.0, 13°C, mutant Y303W
2.5
reduced ferredoxin
-
pH 8.0, 13°C, mutant Y308W
7.7
reduced ferredoxin
-
pH 8.0, 13°C, mutant Y308S
23.9
reduced ferredoxin
-
pH 8.0, 13°C, mutant Y308F
32
reduced ferredoxin
pH 8.0, 13°C, mutant Y303F
58
reduced ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM
70
reduced ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM
90
reduced ferredoxin
-
native enzyme, pH 8.0, 30°C
90 - 174
reduced ferredoxin
-
-
117
reduced ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM
120
reduced ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM
130
reduced ferredoxin
-
mutant lacking pH 8.2, 25°C
135
reduced ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM
139
reduced ferredoxin
-
pH 8.0, 13°C, wild-type enzyme
148
reduced ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 200 mM
155
reduced ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 100 mM
174
reduced ferredoxin
-
recombinant enzyme, pH 8.0, 30°C
176
reduced ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM
192
reduced ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 100 mM
200
reduced ferredoxin
-
above, electron transfer via the enzyme to NADP+
200
reduced ferredoxin
pH 8.0, 13°C, wild-type enzyme
200 - 600
reduced ferredoxin
-
-
200 - 600
reduced ferredoxin
-
-
209
reduced ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM
225
reduced ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 28 mM
260
reduced ferredoxin
-
wild-type, pH 8.2, 25°C
280
reduced ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM
600
reduced ferredoxin
-
electron transfer via the enzyme to NADP+
45
reduced ferredoxin I
-
pH 7.0, 15°C, recombinant chimeric enzyme
-
82
reduced ferredoxin I
-
pH 7.0, 15°C, wild-type leaf isozyme
-
115
reduced ferredoxin I
-
pH 7.0, 15°C, wild-type root isozyme
-
177
reduced ferredoxin I
-
wild-type cofactor, pH 7.5, 25°C
-
32.2
reduced ferredoxin II
-
wild-type cofactor, pH 7.5, 25°C
-
36.8
reduced ferredoxin II
-
ferredoxin mutant D64N pH 7.5, 25°C
-
147
reduced ferredoxin II
-
ferredoxin mutant Q39R/S28E, pH 7.5, 25°C
-
0.004
reduced flavodoxin
-
flavodoxin I or II
0.25
reduced flavodoxin
pH 8.0
2 - 8
reduced flavodoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM
2.5
reduced flavodoxin
pH 8.0, 13°C, mutant Y303W
4
reduced flavodoxin
-
pH 8.0, 13°C, mutant Y308F
7
reduced flavodoxin
pH 8.0, 13°C, mutant Y303F
8.3
reduced flavodoxin
-
pH 8.0, 13°C, mutant Y308W
14
reduced flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM
17
reduced flavodoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM
19
reduced flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM
20
reduced flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM
23.3
reduced flavodoxin
pH 8.0, 13°C, wild-type enzyme
23.3
reduced flavodoxin
-
using cytochrome c as electron acceptor
24
reduced flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 28 mM
25
reduced flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM
25
reduced flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM
26
reduced flavodoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 100 mM
30.6
reduced flavodoxin
-
pH 8.0, 13°C, wild-type enzyme
38
reduced flavodoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM
38.1
reduced flavodoxin
-
mutant bearing a truncated N-terminal domain beginning after the KISKK domain, pH 7.5, temperature not specified in the publication
45.4
reduced flavodoxin
-
mutant bearing lysine to glutamine mutations in the second and third lysine residues of the KISKK domain, pH 7.5, temperature not specified in the publication
65
reduced flavodoxin
-
mutant bearing a lysine to glutamine mutation in the first lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication
66.3
reduced flavodoxin
-
mutant bearing a lysine to glutamine mutation in the second lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication
104
reduced flavodoxin
-
wild-type, pH 7.5, temperature not specified in the publication
128.2
reduced flavodoxin
-
mutant bearing an N-terminal region with the full wheat KISKK domain, pH 7.5, temperature not specified in the publication
139.4
reduced flavodoxin
-
mutant with an extended N-terminal region to include the EAxxPA motif of maize, pH 7.5, temperature not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
low efficiency
-
additional information
additional information
-
low efficiency
-
additional information
additional information
-
the low efficiency is intrinsic to the reductase itself
-
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E139?
-
different conformation
E139D
-
site-directed mutagenesis, altered conformation compared to the wild-type enzyme, slightly reduced activity compared to the wild-type enzyme
E139Q
-
site-directed mutagenesis, mutant enzyme shows increased interaction with ferredoxin and reduces the appropriate orientation of flavodoxin, altered conformation compared to the wild-type enzyme, increased activity compared to the wild-type enzyme
I59A
-
kcat for flavodoxin is slightly decreased, but kcat/Km is markedly increased
I59A/I92A
-
kcat and kcat/Km for flavodoxin are markedly reduced
I59E
-
kcat for flavodoxin is increased, kcat/Km is markedly increased
I59E/I92E
-
kcat and kcat/Km for flavodoxin are markedly reduced
I92A
-
kcat for flavodoxin is increased, kcat/Km is markedly increased
I92E
-
kcat for flavodoxin is increased, kcat/Km is markedly increased
K138E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K290E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K294E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K72E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L263A
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
L263P
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
L76D
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L76F
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L76S
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L76V
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78D
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78F
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78S
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78V
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
R16E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
R224Q/R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
S223D/R224Q/R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
S223D/R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G/A160T
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G/A160T/L263P/R264P/G265P
called PP5, increased Km but reduced kcat for NADPH
T155G/A160T/L263P/R264P/G265P/Y303S
called PP5CT, no protein expressed
T155G/A160T/L263P/Y303S
called PP3CT, catalytic efficiency comparable with wild type, high specificity for NADH
T155G/A160T/S223D/L263P/R264P/G265P
called AMP1PP5, almost no reactivity
T155G/A160T/S223D/R224Q/R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G/A160T/S223D/R224Q/R233L/Y235F/L263P
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G/A160T/S223D/Y235F/L263P/R264P/G265P
called AMP2PP5, almost no reactivity
T155G/R224Q/R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G/S223D/R224Q/R233L/Y235F
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
W57E
-
kcat and kcat/Km for flavodoxin are markedly reduced
W57K
-
kcat and kcat/Km for flavodoxin are markedly increased
W57R
-
kcat for flavodoxin is increased
Y235A
-
reduction of mutant by NADPH is much slower than for wild-type
Y235F
-
reduction of mutant by NADPH similar to wild-type
E301A
-
8% FAD semiquinone at the equilibrium. Mutation does not change quinone substrate specificity but confers the mixed single- and two-electron mechanism of quinone reduction, whereas wild-type uses a single-electron pathway. Change can be explained by the relative increase in the rate of second electron transfer
-
H324F
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
H324S
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R186G
site-directed mutagenesis, replacement of Arg186 with glycine leads to drastically reduced amounts of recombinant protein
R186G/D187H
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R186G/D187H/R190Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
R190Q
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR
K135L
-
site-directed mutagenesis, altered tertiary structure compared to the wild-type enzyme, no methylation at K83, 10% of native wild-type enzyme activity
K83L
-
site-directed mutagenesis, altered tertiary structure compared to the wild-type enzyme, no methylation at K83, 2-4% of native wild-type enzyme activity
K83L/K89L
-
site-directed mutagenesis, altered tertiary structure compared to the wild-type enzyme, no methylation at K83, 0.3% of native wild-type enzyme activity
K89L
-
site-directed mutagenesis, altered tertiary structure compared to the wild-type enzyme, no methylation at K83, 4% of native wild-type enzyme activity
Y308S
mutant uses NAD(H) instead of NADP(H), expression of the mutant has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
Y308F
-
site-directed mutagenesis, about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin
Y308W
-
site-directed mutagenesis, nearly inactive mutant with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
H286A
kcat and kcat/Km are markedly reduced
H286K
considerable decrease in kcat and kcat/Km, almost no reactivity with K3Fe(CN)6
H286L
kcat and kcat/Km are markedly reduced, anomalous reactivity with 2,6-dichlorophenolindophenol
H286Q
up to 50% higher kcat than wild type, higher kcat/Km when 2,6-dichlorophenolindophenol serves as electron acceptor
K259A
50% decrease in catalytic efficiency compared to wild-type
K259D
50% decrease in catalytic efficiency compared to wild-type
K259A
-
50% decrease in catalytic efficiency compared to wild-type
-
K259D
-
50% decrease in catalytic efficiency compared to wild-type
-
A266y/Del267-272
deletion/mutation emulates the structure present in plastidic versions of the protein. It does not modify the general geometry of FAD itself, but increases exposure of the flavin to the solvent, prevents a productive geometry of FAD:NADP(H) complex and decreases the protein thermal stability. Mutant displays higher affinity for NADP+ than wild-type
Del267-272
deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type
S96G
-
shows 2% of wild type activity
S96V
-
shows only 0.05% of wild type activity
DELTA1-15
-
removal of the N-terminal 15 residues of enzyme enhances the interaction with ferredoxin
DELTA81-118
-
deleted amino acid comprise a species-specific subdomain containing an insertion of 28 residues, deletion results in an catalytically active enzyme form with 10fold decreased affinity for ferredoxin
Q242R
-
catalytic activity similar to wild-type. Protein moves faster than wild-type on SDS-PAGE
Q242R/S267R
-
10fold increase in binding affinity for ferredoxin, 1-4% of wild-type activity.
S267R
-
10fold increase in binding affinity for ferredoxin, 1-4% of wild-type activity
S267V
-
no effect on binding of ferredoxin
E19C
-
site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview
E25C
-
site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview
E36C
-
site-directed mutagenesis of isozyme L-FNR I, NADPH-dependent cyt c reduction activity with different recombinant wild-type and mutant ferredoxins, in comparison to the wild-type enzyme, NMR chemical shift perturbation analysis, overview
E139K
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
E139K
-
site-directed mutagenesis, mutant enzyme shows increased interaction with ferredoxin and reduces the appropriate orientation of flavodoxin, altered conformation compared to the wild-type enzyme, increased activity compared to the wild-type enzyme
E301A
-
no significant differences to wild type enzyme
E301A
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
E301A
-
8% FAD semiquinone at the equilibrium. Mutation does not change quinone substrate specificity but confers the mixed single- and two-electron mechanism of quinone reduction, whereas wild-type uses a single-electron pathway. Change can be explained by the relative increase in the rate of second electron transfer
E301A
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
K75E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K75E
-
mutation results in changes of charge distribution on the surface of the protein and in formation of a salt bridge between E75 and K72 that inhibits the essential interaction of these residues with flavodoxin/ferredoxin
R100A
-
amino acid replacement removes the positive charge and the ability to form hydrogen bonds, enzyme interacts weakly with Cibacron-Blue Sepharose, increased Km for NADPH
R100A
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
R100A
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
R264E
-
altered behavior with ferredoxin and flavodoxin
R264E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
T155G/A160T/L263P
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
T155G/A160T/L263P
called PP3, only half catalytic efficiency compared with wild type
Y303F
site-directed mutagenesis, about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
Y303F
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
Y303S
site-directed mutagenesis, inactive mutant
Y303S
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
Y303W
site-directed mutagenesis, nearly inactive mutant
Y303W
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
Y50G
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50G
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity
Y50G
the mutation decreases thermal stability compared to the wild type enzyme
Y50S
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50S
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity
Y50S
the mutation decreases thermal stability compared to the wild type enzyme
Y50W
mutation results in a blue shift of the FAD transition bands, with quenching of fluorescence emission. Mutant displays decreased thermal stability
Y50W
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. The mutant retains approximately 20 % reactivity in the diaphorase assay and BsFd-dependent cytochrome c reduction assay relative to wild-type
Y50W
the mutation decreases thermal stability compared to the wild type enzyme, The mutant retains approximately 20% of wild type reactivity
Y50G
-
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity
-
Y50G
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
Y50S
-
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity
-
Y50S
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
Y50W
-
site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. The mutant retains approximately 20 % reactivity in the diaphorase assay and BsFd-dependent cytochrome c reduction assay relative to wild-type
-
Y50W
-
mutation results in a blue shift of the FAD transition bands, with quenching of fluorescence emission. Mutant displays decreased thermal stability
-
Y308S
-
altered cofactor specificity compared to the wild-type enzyme, mutant enzymes is able to utilizes NADP(H) as well as NAD(H)
Y308S
-
site-directed mutagenesis, about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin
A266Y
mutant does not allow formation of active charge-transfer complexes, probably due to restraints of C-terminus pliability. Mutant displays higher affinity for NADP+ than wild-type
A266Y
site-directed mutagenesis, deletion of the six C-terminal amino acids FVGEGI beyond Ala266 is combined with the replacement A266Y to emulate the structure of plastidic reductases. THe mutations produce subtle global conformational changes, but strongly reduce the local rigidity of the FAD-binding pocket, exposing the isoalloxazine ring to the solvent. Thus, the ultrafast charge-transfer quenching of FAD* by the conserved Tyr66 residue is absent in the mutant series, producing enhancement of the excited singlet and triplet-state properties of FAD. All RcFPR variants display higher affinity for NADP+ than the wild-type
additional information
-
construction of active site mutants
additional information
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
-
isozyme LFNR2 can only partially compensate for the function of LFNR1
additional information
-
construction of in Arabidopsis mutants completely devoid of FNR1 or FNR2
additional information
site-directed mutagenesis of NADPH-specific BsFNR to replace Arg186, Asp187, Arg190, and His324 with the residues occurring in NADH/NADPH-bispecific Chlorobium tepidum FNR
additional information
-
site-directed mutagenesis of NADPH-specific BsFNR to replace Arg186, Asp187, Arg190, and His324 with the residues occurring in NADH/NADPH-bispecific Chlorobium tepidum FNR
additional information
-
replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH. The Y50G and Y50S mutations enhance the FAD fluorescence emission, whereas those of the wild type and Y50W mutant are quenched
additional information
replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH. The Y50G and Y50S mutations enhance the FAD fluorescence emission, whereas those of the wild type and Y50W mutant are quenched
additional information
-
the depletions of residues Y313 to K332 (whole C-terminal extension region) and S325 to K332 results in significant increases in the catalytic efficiency with NADPH in diaphorase assay with ferricyanide, whereas Km values for ferricyanide are increased. In the cytochrome c reduction assay in the presence of ferredoxin, the S325-K332 depleted mutant displays a significant decrease in the turnover rate. The Y313-K332 depleted mutant demonstrates an increase in the rate of the direct reduction of horse heart cytochrome c in the absence of ferredoxin
additional information
-
the depletions of residues Y313 to K332 (whole C-terminal extension region) and S325 to K332 results in significant increases in the catalytic efficiency with NADPH in diaphorase assay with ferricyanide, whereas Km values for ferricyanide are increased. In the cytochrome c reduction assay in the presence of ferredoxin, the S325-K332 depleted mutant displays a significant decrease in the turnover rate. The Y313-K332 depleted mutant demonstrates an increase in the rate of the direct reduction of horse heart cytochrome c in the absence of ferredoxin
-
additional information
-
replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH. The Y50G and Y50S mutations enhance the FAD fluorescence emission, whereas those of the wild type and Y50W mutant are quenched
-
additional information
-
deletions of Tyr326-Glu360 decrease the hydride transfer rate and the amount of reduced enzyme increases at equilibrium relative to wild type. Deletions of Phe337-Glu360 and Ser338-Glu360 result in slight changes in the reaction kinetics and redox equilibrium compared to the wild type enzyme
additional information
-
construction of ferredoxin II mutants Q39R/S28E and D64N by site-directed mutagenesis, expression of recombinant wild-type and mutant ferredoxins of Equisetum arvense in Escherichia coli
additional information
mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. The plastidic enzyme lacking the beta-hairpin is unable to fold properly. An extra tryptophan at the carboxy terminus, emulating the bacterial enzyme, results in an enzyme with decreased affinity for FAD and reduced diaphorase and ferredoxin-dependent cytochrome c reductase activities. The insertion of the beta-hairpin into the corresponding position of the bacterial enzyme increases FAD affinity but does not affect its catalytic properties. The same insertion with simultaneous deletion of the carboxyterminal tryptophan produces a bacterial chimera emulating the plastidic architecture with an increased kcat and an increased catalytic efficiency for the diaphorase activity and a decrease in the enzymes ability to react with its substrates ferredoxin and flavodoxin. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed
additional information
-
addition of an artificial metal binding site of nine amino acids, including four His residues, to the C-terminal Tyr308 residue. The additional structure binds Zn2+ or Co2+ and significantly reduces the catalytic efficiency of the enzyme by decreasing the kcat value. In absence of Zn2+, Km value of NADPH and Kd value for NADP+ are increased 2 to 3 times
additional information
mutual exchange of the 112-123 beta-hairpin from Pisum sativum plastidic ferredoxinNAD(P)H reductase and the carboxy-terminal tryptophan of he Escherichia coli enzyme. The plastidic enzyme lacking the beta-hairpin is unable to fold properly. An extra tryptophan at the carboxy terminus, emulating the bacterial enzyme, results in an enzyme with decreased affinity for FAD and reduced diaphorase and ferredoxin-dependent cytochrome c reductase activities. The insertion of the beta-hairpin into the corresponding position of the bacterial enzyme increases FAD affinity but does not affect its catalytic properties. The same insertion with simultaneous deletion of the carboxyterminal tryptophan produces a bacterial chimera emulating the plastidic architecture with an increased kcat and an increased catalytic efficiency for the diaphorase activity and a decrease in the enzyme's ability to react with its substrates ferredoxin and flavodoxin. Crystallographic structures of the chimeras show no significant changes in their overall structure, although alterations in the FAD conformations are observed
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a tyrosine mutant accepts NAD(H) as cofactor and is insensitive to inhibition by NADH
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construction of 2 different chimeric enzymes with domains of spinach nonphotosynthetic root isozyme and photosynthetic leaf isozyme, the chimera comprising the root NADP-binding domain and the leaf FAD-binding domain is functional, while the chimera with opposite composition is not, the active chimera shows partially impaired intermolecular electron transfer, and highly increased NADPH-diaphorase activity, and increased activity with NADH as cofactor compared to the parent isozymes, improvement of catalytic properties, overview
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study on impact of N-terminal truncation on interaction with ferredoxin using deletions of up to 25 amino acids. Similar kcat values for cytochrome c reduction are measured for all but the most truncated pFNRII[N-5]DEGV which contains a truncated N-terminal domain beginning after the KISKK domain. The longer forms of isoform FNRII bind more strongly to a ferredoxin affinity column than the shorter forms. Mutants bearing lysine-to-glutamine mutations in the KISKK domain are affected in binding to the ferredoxin column
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introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins
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