Ligand ferricyanide

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Basic Ligand Information

Molecular Structure
Picture of ferricyanide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C6FeN6
ferricyanide
CRWNKXHVYMVLCY-UHFFFAOYSA-N
Synonyms:
(Fe(CN)6)3-, Fe(CN)3-, Fe(CN)3[side 2], Fe(CN)6 3-, Fe(CN)63-, ferricyanide[side 2], hexacyanoferrate(III), hexacyanoferrate (III), [Fe(CN)6]3-, [Fe(CN6)]3-

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
taurine + H2O + ferricyanide = 2-sulfoacetaldehyde + NH3 + ferrocyanide
-

Substrate in Enzyme-catalyzed Reactions (220 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
L-lactate + ferricyanide = pyruvate + ferrocyanide + H+
-
show the reaction diagram
D-lactate + ferricyanide = pyruvate + ferrocyanide
-
show the reaction diagram
D-glucose + ferricyanide = 2-dehydro-D-glucose + ferrocyanide
-
show the reaction diagram
polyvinyl alcohol + ferricyanide = polyvinylketone + ferrocyanide
-
show the reaction diagram
D-galactopyranose + ferricyanide = D-galacto-hexodialdose + ferrocyanide
-
show the reaction diagram
D-lactate + ferricyanide = pyruvate + ferrocyanide
-
show the reaction diagram
D-glucose + ferricyanide = D-glucono-1,5-lactone + ferrocyanide
-
show the reaction diagram
sn-glycerol 3-phosphate + ferricyanide = glycerone phosphate + ferrocyanide
-
show the reaction diagram
(R)-Pantolactone + (Fe(CN)6)3- = 2-Dehydropantonolactone + Fe(CN)64-
-
show the reaction diagram
2-dehydro-D-gluconate + ferricyanide = 2,5-didehydro-D-gluconate + ferrocyanide
-
show the reaction diagram
(R)-lactate + ferricyanide = pyruvate + ferrocyanide
-
show the reaction diagram
H2O + ferricyanide + hv = O2 + ferrocyanide
-
show the reaction diagram
ferricyanide + H2O2 = ferrocyanide + H2O
-
show the reaction diagram
H2 + ferricyanide = H+ + ferrocyanide
-
show the reaction diagram
3-indolemethanol + ferricyanide = ?
-
show the reaction diagram
4-hydroxybenzoate + NADPH + ferricyanide = protocatechuate + NADP+ + ferrocyanide
-
show the reaction diagram
[methionine synthase]-cob(II)alamin + S-adenosyl-L-methionine + ferricyanide = [methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + ?
-
show the reaction diagram
formate + ferricyanide = CO2 + ferrocyanide
-
show the reaction diagram
formate + ferricyanide = CO2 + ferrocyanide + H+
-
show the reaction diagram
NADH + Fe(CN)63- = NAD+ + Fe(CN)64-
-
show the reaction diagram
ferricyanide + NADH = ferrocyanide + NAD+ + H+
-
show the reaction diagram
NADH + H+ + Fe(CN)63- = NAD+ + Fe(CN)62-
-
show the reaction diagram
ferricyanide + NADH = ferrocyanide + NAD+ + H+
-
show the reaction diagram
pyruvate + CoA + ferricyanide = acetyl-CoA + CO2 + ferrocyanide
-
show the reaction diagram
pyruvate + phosphate + ferricyanide + H2O = acetyl phosphate + ferrocyanide + H2O2
-
show the reaction diagram
ferricyanide + O2 = ? + H2O
-
show the reaction diagram
succinate + ferricyanide = fumarate + ferrocyanide
-
show the reaction diagram
succinate + ferricyanide = fumarate + ferrocyanide
-
show the reaction diagram
ferricyanide + NADPH + H+ = ferrocyanide + NADP+
-
show the reaction diagram
taurine + H2O + ferricyanide = 2-sulfoacetaldehyde + NH3 + ferrocyanide
-
show the reaction diagram
NADH + H+ + ferricyanide = NAD+ + ferrocyanide
-
show the reaction diagram
L-proline + ferricyanide + H2O = (S)-1-pyrroline-5-carboxylate + ferrocyanide
-
show the reaction diagram
N6-(2-isopentenyl)adenine 9-beta-D-riboside + ferricyanide + H2O = adenine 9-beta-D-riboside + 3-methylbut-2-enal + ferrocyanide
-
show the reaction diagram
L-proline + ferricyanide = DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
show the reaction diagram
Fe(CN)6 3- + NADPH = Fe(CN)6 4- + NADP+
-
show the reaction diagram
NADH + Fe(CN)63- = NAD+ + Fe(CN)63-
-
show the reaction diagram
hydroxylamine + ferricyanide = nitrite + ferrocyanide + H+
-
show the reaction diagram
ferricyanide + NADPH + H+ = ferrocyanide + NADP+
-
show the reaction diagram
thiosulfate + ferricyanide = tetrathionate + ferrocyanide
-
show the reaction diagram
sulfite + ferricyanide = sulfate + ferrocyanide
-
show the reaction diagram
2 thiosulfate + ferricyanide = tetrathionate + ferrocyanide
-

Product in Enzyme-catalyzed Reactions (36 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
allyl alcohol + ferricyanide = acrolein + ferricyanide
-
show the reaction diagram
ferrocyanide + H2O2 = ferricyanide + H2O
-
-
show the reaction diagram
ferrocyanide + H+ + H2O2 = ferricyanide + H2O
-
-
show the reaction diagram
ferrocyanide + H2O2 = ferricyanide + OH-
-
-
show the reaction diagram
Fe(CN)62- + NAD+ = Fe(CN)63- + NADH + H+
-
-
show the reaction diagram
succinate + ferrocyanide = fumarate + ferricyanide
-
-
show the reaction diagram
NADH + Fe(CN)63- = NAD+ + Fe(CN)63-
-

Enzyme Cofactor/Cosubstrate (5 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (9 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (25 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
inhibition at 0.001 mM, activation at 1 mM
-
0.82 mM, 50% inhibition of brominating activity
-
1 mM, inactivates Fe-MndD
-
1 mM, inactivates Fe-HPCD
-
2.5 mM, 80% decrease in activity within 10 min
-
enzyme a, b, c and e
-
at concentrations above 3 mM
-
inhibition of the recombinant FAD domain
-
irreversible inactivation of molybdenum center
-
inhibition of O2 consumption
-
addition of 0.2 mM ferricyanide causes a rapid oxidation of the enzyme
-
0.05 mM, complete inhibition
-
2 mM, 17% inhibition
-
partial, 28% inhibition
-
blue light irradiation converts fully oxidized FAD to the semiquinone state, but in the presence of ferricyanide as electron acceptor further photoreduction to the fully reduced catalytically active form FADH- is inhibited
-
complete loss of activity
-
inhibits the interaction of the oxidized enzyme with NADH
-

Metals and Ions (4 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
can substitute for cytochrome c
-
not suitable as electron acceptor
-
stimulates
-

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (124 results)

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COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.3
-
fast reaction phase
162
-
slow reaction phase
93
-
apparent turnover number
230
-
at 25°C
12.8
-
at 45°C
24.1
-
cellobiose as substrate, pH 3.5
61
-
pH 7.5, 40°C
14
-
pH 7.5, 25°C
550
-
variant I22/S175
8.24
-
cosubstrate xanthine
18.2
-
recombinant enzyme, pH 8.2, 25°C, with NADH
42
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
63
-
pH 8.5, 30°C
60.2
-
mutant K387A, pH 7.5, 25°C
772
-
mutant K409A, pH 7.5, 25°C
755
-
mutant N384A, pH 7.5, 25°C
898
-
mutant R310A, pH 7.5, 25°C
1485
-
mutant R310E, pH 7.5, 25°C
790
-
mutant R339A, pH 7.5, 25°C
543
-
mutant R65A, pH 7.5, 25°C
560
-
wild-type, pH 7.5, 25°C
982
-
pH 7.2, 30°C
33.7
-
pH 7.5, 30°C
26.8
-
with activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication
883
-
without activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication
60
-
mutant R28E/E29I, pH 8.0, 30°C
26.4
-
mutant R28L, pH 8.0, 30°C
27.1
-
mutant R28L/E29L, pH 8.0, 30°C
28.9
-
mutant R28L/R81A, pH 8.0, 30°C
20.1
-
mutant R28N, pH 8.0, 30°C
24.6
-
mutant R81A, pH 8.0, 30°C
28.1
-
mutant R81E, pH 8.0, 30°C
27.3
-
mutant R81K, pH 8.0, 30°C
30.4
-
wild-type, pH 8.0, 30°C
28.7
-
-
157
-
of NADPH:acceptor oxidoreductase acitivity of the beta subunit of the enzyme
41.9
-
of NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, co-substrate: NADPH, inhibitor: 2'-phosphoadenosine-5'-diphospho-5'beta-D-ribose
39.5
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
21.7
-
DELTAF272 mutant enzyme
400
-
enzyme from erythrocyte cytosol
700
-
enzyme from erythrocyte membrane
677
-
enzyme from liver microsomes, detergent solubilized
827
-
enzyme from liver microsomes, protease solubilized
98.3
-
G273 mutant enzyme
76
-
H49A mutant enzyme
470
-
H49E mutant enzyme
110
-
H49K mutant enzyme
490
-
H49Y mutant enzyme
727
-
K110A mutant enzyme
270
-
K110E mutant enzyme
120
-
K110H mutant enzyme
340
-
K110Q mutant enzyme
40
-
K110R mutant enzyme
470
-
L148P mutant enzyme, pH 7.0, 25°C
300
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
357
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
30.8
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
399
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
504
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
838
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
1241
-
mutant G179A, pH 7.0
559
-
mutant G179P, pH 7.0
42
-
mutant G179T, pH 7.0
33
-
mutant G179V, pH 7.0
12
-
mutant G75S
133
-
mutant G75S/V252M
187
-
mutant P247A
357
-
mutant P247L
30.8
-
mutant P248A
399
-
mutant P248L
504
-
mutant P249A
838
-
mutant P249L
1241
-
mutant P92A, pH 7.0, 25°C
517
-
mutant P92G, pH 7.0, 25°C
467
-
mutant P92S, pH 7.0, 25°C
880
-
mutant V252M
633
-
mutant Y93A, pH 7.0, 25°C
200
-
mutant Y93D, pH 7.0, 25°C
83
-
mutant Y93F, pH 7.0, 25°C
483
-
mutant Y93H, pH 7.0, 25°C
83
-
mutant Y93S, pH 7.0, 25°C
133
-
mutant Y93W, pH 7.0, 25°C
83
-
native enzyme
630
-
P144L mutant enzyme, pH 7.0, 25°C
283
-
P144L/L148P mutant enzyme, pH 7.0, 25°C
100
-
pH 7.0, 25°C
767
-
pH 7.0, 25°C, wild type enzyme
822
-
pH 7.0, 25°C,T66A mutant enzyme
684
-
pH 7.0, 25°C,T66S mutant enzyme
976
-
pH 7.0, 25°C,T66V mutant enzyme
77
-
pH 7.0, S127P mutant enzyme
300
-
pH 7.0, wild type enzyme
800
-
recombinant wild-type enzyme
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
337
-
wild type enzyme, pH 7.0, 25°C
800
-
wild-type
800
-
wild-type, pH 7.0
800
-
wild-type, pH 7.0, 25°C
800
-
-
64.5
-
at pH 7.5 and 25°C
isoform CPR1, at pH 7.6 and 25°C
80
-
mutant enzyme H322A, at pH 7.5 and 25°C
18.1
-
mutant enzyme H322Q, at pH 7.5 and 25°C
26.1
-
wild type enzyme, at pH 7.5 and 25°C
43.5
-
pH 7.0, 25°C, functional FAD-containing domain
1300
-
-
618
-
pH 7.8, temperature not specified in the publication
111
-
-
17000
-

KM Value (168 results)

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COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
6
-
pH 5.5, isoform with activity maximum at pH 5.5
0.07
-
pH 7.5, isoform with activity maximum at pH 7.5
0.138
-
pH 9.5, isoform with activity maximum at pH 9.5
0.27
-
wild type enzyme
0.07
-
Y254F mutant
0.04
-
Y254L mutant
0.03
-
-
0.23
-
substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
3.43
-
slow reaction phase
pH 8.8, 25°C
0.69
-
-
0.55
-
isolated subunit I
0.025
-
-
0.69
-
apparent KM-value
65
-
at 25°C
0.0045
-
at 45°C
0.0067
-
at pH 4.5 and 25°C
0.0045
-
at pH 4.5 and 45°C
0.0067
-
cellobiose as substrate, pH 3.5
0.011
-
pH 7.5, 40°C
0.012
-
at 30°C with 25 mM glucose as susbtrate
0.33
-
-
2.5
-
at pH 6.5 and 30°C
3.87
-
variant I22/S175
formate dehydrogenase I, reaction with formate
0.46
-
formate dehydrogenase I, reaction with NADH
0.69
-
formate dehydrogenase II, reaction with formate
0.5
-
formate dehydrogenase II, reaction with NADH
0.62
-
with 3-phenyl-1-propene as cosubstrate, at pH 7.5 and 25°C
0.362
-
with 3-phenyl-1-propyne as cosubstrate, at pH 7.5 and 25°C
0.77
-
with ethylbenzene as cosubstrate, at pH 7.5 and 25°C
0.028
-
-
0.055
-
at pH 7.0 and 25°C
0.29
-
recombinant enzyme, pH 8.2, 25°C, with NADH
0.015
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
0.022
-
mutant K387A, pH 7.5, 25°C
0.044
-
mutant K409A, pH 7.5, 25°C
0.036
-
mutant N384A, pH 7.5, 25°C
0.043
-
mutant R310A, pH 7.5, 25°C
0.143
-
mutant R310E, pH 7.5, 25°C
0.04
-
mutant R339A, pH 7.5, 25°C
0.045
-
mutant R65A, pH 7.5, 25°C
0.05
-
wild-type, pH 7.5, 25°C
0.04
-
pH 7.2, 30°C
0.16
-
pH 7.5, 30°C
0.0236
-
as electron acceptor under aerobic conditions
0.03
-
-
0.3
-
pH 6.0
0.001
0.002
pH 8.5, 70°C
0.344
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.14
-
at pH 6.4 and 25°C
0.345
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.008
-
DELTAF272 mutant enzyme
0.0052
-
G273 mutant enzyme
0.0052
-
H49A mutant enzyme
0.0028
-
H49E mutant enzyme
0.0022
-
H49K mutant enzyme
0.0006
-
H49Y mutant enzyme
0.0026
-
in the presence of 2 mM Ca2+
0.0136
-
K110A mutant enzyme
0.38
-
K110E mutant enzyme
0.37
-
K110H mutant enzyme
0.05
-
K110Q mutant enzyme
0.76
-
K110R mutant enzyme
0.005
-
L148P mutant enzyme, pH 7.0, 25°C
0.008
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.01096
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.00104
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.01563
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.01568
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.02646
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.03309
-
mutant G179A, pH 7.0
0.008
-
mutant G179P, pH 7.0
0.007
-
mutant G179T, pH 7.0
0.008
-
mutant G179V, pH 7.0
0.007
-
mutant G75S
0.007
-
mutant G75S/V252M
0.008
-
mutant P247A
0.01096
-
mutant P247L
0.00104
-
mutant P248A
0.01563
-
mutant P248L
0.01568
-
mutant P249A
0.02646
-
mutant P249L
0.03309
-
mutant P275L, 25°C, pH 7.0
0.006
-
mutant P92A, pH 7.0, 25°C
0.0074
-
mutant P92G, pH 7.0, 25°C
0.008
-
mutant P92S, pH 7.0, 25°C
0.0078
-
mutant V252M
0.007
-
mutant Y93A, pH 7.0, 25°C
0.0086
-
mutant Y93D, pH 7.0, 25°C
0.0083
-
mutant Y93F, pH 7.0, 25°C
0.0066
-
mutant Y93H, pH 7.0, 25°C
0.0083
-
mutant Y93S, pH 7.0, 25°C
0.0058
-
mutant Y93W, pH 7.0, 25°C
0.0068
-
native enzyme
0.0025
-
P144L mutant enzyme, pH 7.0, 25°C
0.008
-
P144L/L148P mutant enzyme, pH 7.0, 25°C
0.008
-
pH 7.0, 25°C
0.008
-
pH 7.0, 25°C, wild type enzyme
0.0025
-
pH 7.0, 25°C,T66A mutant enzyme
0.0022
-
pH 7.0, 25°C,T66S mutant enzyme
0.0031
-
pH 7.0, 25°C,T66V mutant enzyme
0.0016
-
pH 7.0, S127P mutant enzyme
0.008
-
pH 7.0, wild type enzyme
0.007
-
recombinant enzyme
0.007
-
recombinant wild-type enzyme
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.00723
-
wild type enzyme, pH 7.0, 25°C
0.008
-
wild-type
0.006
-
wild-type, 25°C, pH 7.0
0.007
-
wild-type, pH 7.0
0.008
-
wild-type, pH 7.0, 25°C
0.0071
-
at pH 7.4 and 25°C
0.1193
-
ionic strength: 200 mM
0.035
-
ionic strength: 50 mM
0.021
-
recombinant FAD domain
0.034
-
recombinant flavin domain of nitrate reductase C17S mutant
0.045
-
recombinant flavin domain of nitrate reductase C54S mutant
0.036
-
wild-type recombinant flavin domain of nitrate reductase
0.027
-
pH 7.8, temperature not specified in the publication
0.0009
-
pH 8.0
0.02
-
reaction with ferricyanide or cytochrome c
0.58
-
S0.5 value, pH 4.0, 30°C
0.66
-
S0.5 value, pH 4.0, 42°C
0.18
-
80°C, pH 6.0
3.4
-

Ki Value (3 results)

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COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
25°C, pH 8.2, cosubstrate NADH
0.185
-
25°C, pH 8.2, cosubstrate NADPH
0.23
-
inhibition of the recombinant FAD domain
23
-

References & Links

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Links to other databases for ferricyanide

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ChEBI
PubChem
-
PubChem