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0.241
2-chloro-p-phenylenediamine
-
-
0.161
2-methoxy-p-phenylenediamine
-
-
0.213
2-methyl-p-phenylenediamine
-
-
0.00126
2-nitro-p-phenylenediamine
-
-
0.00262
2-sulfonic acid-p-phenylenediamine
-
-
0.00285
3,4-Dihydroxyphenethylamine
-
-
0.0603
4-methylcatechol
-
-
0.0015
4-phenylenediamine
-
pH 5, 20°C
0.00834
5-hydroxyindol-3-ylacetic acid
-
-
0.908
5-hydroxytryptamine
-
-
0.0163
5-hydroxytryptophan
-
-
0.0051
5-hydroxytryptophol
-
-
0.0035
chlorpromazine
-
-
0.0021
Ferrous ammonium sulfate
-
pH 5.0, 22°C
0.018 - 30.5
hydroquinone
0.00255 - 5.8
L-epinephrine
0.00281
L-norepinephrine
-
-
0.036
m-phenylenediamine
-
-
0.06 - 0.164
N,N'-dimethyl-p-phenylenediamine
0.197
N,N,N',N'-tetramethyl-p-phenylenediamine
-
-
0.556
N,N-diethyl-p-phenylenediamine
-
-
0.00305
N,N-dimethyl-m-phenylenediamine
-
-
0.203
N,N-Dimethyl-p-phenylenediamine
-
-
0.021
N-(p-methoxyphenyl)p-phenylenediamine
-
-
0.0123
N-acetyl-p-phenylenediamine
-
-
0.11
N-ethyl-N-(2-hydroxyethyl)p-phenylenediamine
-
-
0.087
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine
-
-
0.048
N-phenyl-p-phenylenediamine
-
-
0.00288
o-aminophenol
-
-
0.12 - 0.76
o-Dianisidine
0.00295 - 4.15
o-phenylenediamine
0.00154
p-Aminophenol
-
-
0.005 - 2.5
p-phenylenediamine
0.0028
Trifluoperazine
-
-
additional information
additional information
-
0.0006
Fe(II)
pH 6.5, 30°C, 2 Km-values: 0.0006 and 0.050 mM
0.0049
Fe(II)
-
wild-type, pH 6.0
0.0054
Fe(II)
pH 5.0, temperature not specified in the publication
0.0083
Fe(II)
pH 5.0, temperature not specified in the publication
0.0188
Fe(II)
-
mutant D409A, pH 6.0
0.0193
Fe(II)
-
mutant D283A, pH 6.0
0.0356
Fe(II)
-
mutant E185A, pH 6.0
0.04
Fe(II)
recombinant wild-type enzyme, pH 5.0, 25°C
0.05
Fe(II)
pH 6.5, 30°C, 2 Km-values: 0.0006 and 0.050 mM
0.12
Fe(II)
pH 5.0, 23 °C, wild-type enzyme
0.135
Fe(II)
pH 5.0, 23 °C, mutant enzyme M358S/M361S/M362S/M364S/M366S
3.994
Fe(II)
-
mutant E185A/D409A, pH 6.0
0.0006
Fe2+
-
pH 6.5, 30°C, 2 Km-values: 0.0006 and 0.050 mM
0.0035
Fe2+
-
pH 5, 20°C, Km for high-affinity iron-binding sites using a two-component Eadie-Hofstee plot, Vmax: 67 nmol/min
0.0048
Fe2+
-
wild-type, pH 6.0
0.0058
Fe2+
-
mutant Y354F, pH 6.0
0.0079
Fe2+
-
recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication
0.0086
Fe2+
-
mutant E185D, pH 6.0
0.0107
Fe2+
-
pH 5, 20°C, Km for low-affinity iron-binding sites using a two-component Eadie-Hofstee plot, Vmax: 286 nmol/min
0.0108
Fe2+
-
recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication
0.011
Fe2+
-
mutant D278A, pH 6.0
0.017
Fe2+
-
mutant Y354A, pH 6.0
0.04
Fe2+
-
mutant E185A, pH 6.0
0.046
Fe2+
-
xanthine oxidoreductase with ferroxidase activity
0.05
Fe2+
-
pH 6.5, 30°C, 2 Km-values: 0.0006 and 0.050 mM
1.43
Fe2+
-
recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication
3
Fe2+
-
wild-type, pH 6.5, 4°C
3.51
Fe2+
-
mutant E185A/Y354A, pH 6.0
4.6
Fe2+
-
mutant Y354A, pH 6.5, 4°C
8.2
Fe2+
-
mutant E185D, pH 6.5, 4°C
12.7
Fe2+
-
mutant Y354F, pH 6.5, 4°C
14.1
Fe2+
-
mutant E185A, pH 6.5, 4°C
0.018
hydroquinone
-
mutant E185A
0.019
hydroquinone
-
mutant D283A
0.025
hydroquinone
-
wild-type
0.03
hydroquinone
-
mutant D409A
0.03
hydroquinone
-
mutant E185A/D409A
3
hydroquinone
-
wild-type, pH 6.0
3
hydroquinone
-
wild-type, pH 6.5, 25°C
4.3
hydroquinone
-
mutant D278A, pH 6.0
4.6
hydroquinone
-
mutant Y354A, pH 6.0
4.6
hydroquinone
-
mutant Y354A, pH 6.5, 25°C
8.2
hydroquinone
-
mutant E185D, pH 6.0
8.2
hydroquinone
-
mutant E185D, pH 6.5, 25°C
12.7
hydroquinone
-
mutant Y354F, pH 6.0
12.7
hydroquinone
-
mutant Y354F, pH 6.5, 25°C
14.1
hydroquinone
-
mutant E185A, pH 6.0
14.1
hydroquinone
-
mutant E185A, pH 6.5, 25°C
16.9
hydroquinone
-
mutant E185A/Y354A, pH 6.0
18.2
hydroquinone
-
mutant E185A, pH 6.0
19.3
hydroquinone
-
mutant D283A, pH 6.0
25.5
hydroquinone
-
wild-type, pH 6.0
30.3
hydroquinone
-
mutant D409A, pH 6.0
30.5
hydroquinone
-
mutant E185A/D409A, pH 6.0
0.00255
L-epinephrine
-
-
0.06
N,N'-dimethyl-p-phenylenediamine
-
-
0.11
N,N'-dimethyl-p-phenylenediamine
-
-
0.164
N,N'-dimethyl-p-phenylenediamine
-
-
0.14
NADH
-
pH 6.0, 30°C, presence of triflupromazine
0.21
NADH
-
pH 6.0, 30°C, presence of levomepromazine
0.22
NADH
-
pH 6.0, 30°C, presence of chlorpromazine
0.23
NADH
-
pH 6.0, 30°C, presence of promazine
0.12
o-Dianisidine
-
-
0.00295
o-phenylenediamine
-
-
4.15
o-phenylenediamine
-
-
0.0011
O2
-
-
0.0074
O2
pH 7.0, 30°C, 0.2 M phosphate buffer
0.0182
O2
pH 7.0, 30°C, 0.2 M acetate buffer
0.0276
O2
pH 5.2, 30°C, 0.0133 M phosphate buffer
0.0286
O2
pH 5.4, 30°C, 0.2 M acetate buffer
0.05
O2
-
xanthine oxidoreductase with ferroxidase activity
0.0554
O2
pH 6.3, 30°C, 0.0133 M phosphate buffer
0.0632
O2
pH 6.5, 30°C, 0.2 M acetate buffer
0.005
p-phenylenediamine
-
mutant D278A, pH 6.0
0.008
p-phenylenediamine
-
mutant Y354A, pH 6.0
0.0084
p-phenylenediamine
-
wild-type, pH 6.0
0.0143
p-phenylenediamine
-
mutant Y354F, pH 6.0
0.019
p-phenylenediamine
-
-
0.0228
p-phenylenediamine
-
mutant E185D, pH 6.0
0.0333
p-phenylenediamine
-
mutant E185A, pH 6.0
0.053
p-phenylenediamine
-
-
0.0705
p-phenylenediamine
-
mutant E185A/Y354A, pH 6.0
0.085
p-phenylenediamine
-
-
0.22
p-phenylenediamine
-
-
0.292
p-phenylenediamine
-
-
0.36
p-phenylenediamine
-
-
0.64
p-phenylenediamine
-
-
0.78 - 2.5
p-phenylenediamine
-
-
0.9
p-phenylenediamine
-
-
1.1
p-phenylenediamine
-
-
1.12
p-phenylenediamine
-
-
1.19
p-phenylenediamine
-
-
additional information
additional information
Thermosynechococcus vestitus
iron oxidation and incorporation kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics and steady-state turnover of Fe2+, overview
-
additional information
additional information
-
steady-state kinetics of iron mineralization and of Fe(II) oxidation and thermodynamics, overview
-
additional information
additional information
stopped-flow kinetics and initial velocities of iron oxidation of wild-type and mutant enzymes, overview
-
additional information
additional information
-
stopped-flow kinetics and initial velocities of iron oxidation of wild-type and mutant enzymes, overview
-
additional information
additional information
kinetics of Fe(II) oxidation of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of Fe(II) oxidation of wild-type and mutant enzymes
-
additional information
additional information
-
network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms, allosteric mechanisms observed among homologous proteins, overview
-
additional information
additional information
-
network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms, allosteric mechanisms observed among homologous proteins, overview
-
additional information
additional information
-
stopped-flow kinetics and single-turnover oxidoreductase kinetics, measuring diferric-peroxo intermediate and Fe3+
-