Ligand ferricyanide

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

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)

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)

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)

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)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (9 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (25 results)

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)

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)

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)

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)

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

Links to other databases for ferricyanide

ChEBI
PubChem
-
PubChem