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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
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-
0.0022
reduced ferredoxin
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at pH 7.5 and 20°C
0.0022
reduced ferredoxin
-
at pH 7.5 and 25°C
0.0023
reduced ferredoxin
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at pH 7.5 and 15°C
0.0024
reduced ferredoxin
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at pH 7.5 and 30°C
0.0026
reduced ferredoxin
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native enzyme, pH 8.0, 30°C
0.0028
reduced ferredoxin
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mutant lacking amino acids 81 to 118, pH 8.2, 25°C
0.0038
reduced ferredoxin
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enzyme II
0.0043
reduced ferredoxin
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enzyme I
0.0045 - 0.0046
reduced ferredoxin
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ferredoxin-dependent cytochrome c reductase activity
0.005
reduced ferredoxin
-
-
0.0058
reduced ferredoxin
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pH 8.0, 13°C, mutant Y308F
0.0065
reduced ferredoxin
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pH 8.0, 13°C, wild-type enzyme
0.0066
reduced ferredoxin
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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
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wild-type, pH 8.2, 25°C
0.051
reduced ferredoxin
pH 8.0, 13°C, mutant Y303F
0.0025
reduced ferredoxin I
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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
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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increasing NH4Cl concentration enhances Km
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additional information
additional information
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enzyme reacts slower with different mutants of ferredoxin than with wild type ferredoxin
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additional information
additional information
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Km value of different mutants
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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Km value increases with pH
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additional information
additional information
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enzyme covalently cross-linked to flavodoxin
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additional information
additional information
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increasing light intensity reduces Km
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additional information
additional information
kinetics, wild-type and mutant enzymes
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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below 0.1 mM, oxidized ferredoxin with NADH, pH 7.0, 24°C
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additional information
additional information
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detailed binding kinetics, detailed reaction kinetics, enzyme-substrate complex formation
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
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additional information
additional information
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gradual decrease in activity according to biphasic kinetics within 120 min
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additional information
additional information
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kinetics, rapid thermal inactivation of reduced enzyme and drop of activity
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additional information
additional information
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steady-state kinetics and dissociation constants of NADPH-enzyme complex, wild-type isozymes and recombinant chimera
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additional information
additional information
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stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes
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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
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additional information
additional information
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stopped-flow kinetics measurements, pH 8.0, 13°C, steady-state kinetics for wild-type and mutant enzymes dependent on ionic strength, overview
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additional information
additional information
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thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
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additional information
additional information
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
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additional information
additional information
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Michaelis-Menten kinetics, overview
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additional information
additional information
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analysis of kinetic rate constants for the reaction of enzyme with NADP+/NADPH
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additional information
additional information
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Fpr showed high specificity for NADPH; Km value for NADPH is <5 microMol, whereas that for NADH is above 2 mM
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additional information
additional information
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stopped flow kinetic analysis
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additional information
additional information
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Stopped-flow pre-steady-state kinetics, overview
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additional information
additional information
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kinetic evidence for its bifurcating behavior of the enzyme, cofactor kinetics, overview
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additional information
additional information
spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview
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additional information
additional information
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spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview
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