Ligand Fe3+

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Basic Ligand Information

Molecular Structure
Picture of Fe3+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Fe
Fe3+
VTLYFUHAOXGGBS-UHFFFAOYSA-N
Synonyms:
cytochrome c-550, cytochrome c550, Fe(III), Fe(III)[side 2], Fe3+[side 2]


Show all pahtways known for Show all BRENDA pathways known for Fe3+

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
alcohol + cytochrome c550 = aldehyde + reduced cytochrome c550
show the reaction diagram
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NADH + Fe3+ = NAD+ + Fe2+
show the reaction diagram
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ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+
show the reaction diagram
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ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
show the reaction diagram
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ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (178 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
protoporphyrin IX + ascorbate + O2 = hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
-
-
Fe(II) + rusticyanin = Fe(III) + reduced rusticyanin
show the reaction diagram
-
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (80 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
alcohol + cytochrome c550 = aldehyde + reduced cytochrome c550
show the reaction diagram
-
2 Fe3+ + 3 ferrozine + NADH = 2 Fe(II)-ferrozine + NAD+ + H+
show the reaction diagram
-
NADH + Fe3+ = NAD+ + Fe2+
show the reaction diagram
-
ferrocytochrome c + Fe3+ = ferricytochrome c + Fe2+
show the reaction diagram
-
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (299 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
protoporphyrin IX + ascorbate + O2 = hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
-
-
2 Fe(II) + NADP+ + H+ = 2 Fe(III) + NADPH
show the reaction diagram
-
-
Fe2+ + O2 + H+ = Fe3+ + H2O
show the reaction diagram
-
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-
-
ATP + H2O + Fe3+/out = ADP + phosphate + Fe3+/in
show the reaction diagram
-

Enzyme Cofactor/Cosubstrate (2 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (47 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
pMMO, optimal at 5.0 mM
-
0.5 microM Fe(III)-citrate and 0.5 microM Fe(III)-EDTA induces Fprs
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10 mM, 115% of initial activity
-
stimulates galactosaminidase activitiy of form I
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Inhibitor in Enzyme-catalyzed Reactions (1347 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM inhibits entirely
-
1mM, 29% residual activity
-
1 mM, 74% residual activity
-
11% inhibition at 1 nM
-
0-15% inactivation at 1 mM
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
0.5 mM, strong inhibition
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1 mM, 2% of initial activity with substrate diacetyl, 3.5% with substrate 2,3-butanediol, respectively
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strong inhibition at 0.5 mM
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complete inhibition at 5 mM
-
enzyme activities are significantly decreased in the presence of 30 and 300 ppm Fe3+
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27.2% residual activity at 5 mM
-
strong inhibition
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0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
18% residual activity at 1 mM
-
1 mM, 30% residual activity
-
inhibits diacetyl and (3S/3R)-acetoin reduction
-
1 mM, 44% residual activity
-
0.5 mM, 68% of initial activity
-
complete inhibition at 10 mM
-
73% residual activity at 1 mM
-
1 mM, 91% inhibition
-
90% inhibition at 0.1 mM
-
95% inhibition at 0.1 mM
-
complete inhibition at 1 mM
-
inhibits the light emission by dinoflagellate luciferase
-
slight inhibition
-
less than 10% activity at 1 mM
-
2 mM, 68% residual activity
-
1 mM, 56% inhibition
-
1 mM, moderate inhibition
-
0.1 mM, 77% residual activity
-
slight effect, crude enzyme extract
-
3% residual activity at 1 mM
-
0.1 mM inhibits by 23%, 1 mM completely inhibits; complete inhibition at 1 mM
-
2 mM, 67% loss of activity
-
5 mM, 65% inhibition
-
83.5% inhibition at 1 mM
-
complete inhibition at 1 mM
-
1 mM causes complete inhibition
-
10 mM FeCl3, 80% inhibition
-
0.1 mM, 15% residual activity
-
10 mM concentration 35% inhibition
-
91% residual activity at 2 mM Fe3+
-
10 mM, 85% inhibition of reductive amination
-
1 mM, no residual activity
-
0.5 mM, 8% inhibition at pH 8.9, no effect on activity at pH 7.8
-
about 42% residual activity at 1 mM
-
complete inhibition at 1 mM
-
10.78% residual activity at 3 mM
-
2.85 mM, 26% inhibition of pyridoxamine 5'-phosphate oxidation, 50% inhibition of pyridoxine oxidation
-
less potent inhibitor, effect cannot reversed by EDTA
-
14% inhibition at 0.05 mM
-
1 mM, 85% inhibition
-
strong inhibition
-
competitive
-
1 mM, complete inhibition
-
48% inhibition at 1 mM
-
5 mM, complete inhibition
-
complete inhibition at 5 mM
-
5 mM, strong inhibition
-
5 mM, more than 90% inhibition
-
5 mM, more than 90% inhibition
-
5 mM, more than 95% inhibition
-
14% inhibition by 5 mM
-
quantum mechanical/molecular mechanical dynamics study
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5 mM chloride salt, strong inhibitory effect, 50-100%, PpSABATH1
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18% inhibition at 2 mM
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at higher concentrations
-
20 ng/ml medium, 30% inhibition of the free enzyme, 22% inhibition of the immobilized enzyme
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0.4 mM
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32% inhibition at 10 mM; 32% inhibition at 10 mM
-
1 mM inhibits
-
enzymatic activity is abolished in the presence of Fe3+
-
0.5 mM, 83% inhibition
-
complete inhibition at 10 mM
-
1 mM, 82% residual acitvity
-
60.78% residual activity at 5 mM
-
inhibits Mn2+-activated enzyme, 0.03 mM: 27% inhibition of activity with 0.01 mM Mn2+ and 0.035 mM UDP-glucose
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72% inhibition at 1 mM
-
1 mM, 65% inhibition of hydrolysis reaction, 15% inhibition of transfer reaction
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strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
-
84% inhibition at 0.1 mM
-
Lyn or Hck kinases in the unphosphorylated active state are significantly inhibited by Fe3+ ion
-
56% inhibition at 10 mM
-
13.7% residual activity at 5 mM
-
35% residual activity at 1 mM
-
3.3% residual activity at 1 mM
-
strong inhibition, 98% inhibition at 10 mM
-
plasmalogen-specific PLA2
-
strong inhibition at 1 mM
-
strong inhibition at 1 mM
-
10 mM, 43% residual acivity
-
5 mM, 38% loss of activity
-
41% of maximal activity at 1 mM FeCl3
-
strong inhibition
-
complete inhibition at 0.1 mM
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
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