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Ligand 1,10-phenanthroline

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Basic Ligand Information

Molecular Structure
Picture of 1,10-phenanthroline (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C12H8N2
1,10-phenanthroline
DGEZNRSVGBDHLK-UHFFFAOYSA-N
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Synonyms:
1,10 phenanthroline, 1,10-o-phenanthroline, 1,10-ophenanthroline, 1,10-ortho-phenanthroline, 1,10-phenantroline, o-phenanthroline, o-phenanthroline hydrate, o-Phenantroline, o-Phenathroline, o-Phenynthroline, ortho-phenanthroline, orthophenanthroline

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (2 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
propyl-2-nitronate + Cu(0) + 1,10-phenanthroline + O2 = propan-2-one + ?
show the reaction diagram
-
3'-phosphoadenylylsulfate + 1,10-phenanthroline = adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (32 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
at 1.85 mM 135% of the activity without activator
-
123% activity at 1 mM
-
activates to 108% activity compared to the control activity at 0.1 mM and to 109% at 1 mM
-
activates to 108% activity compared to the control activity at 0.1 mM and to 109% at 1 mM
-
1 mM, 1.25fold activation
-
stimulation
-
slightly activates, chelates Mn3+
-
similar stimulating effect as 2,2' dipyridyl
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stimulates if it reaches an equimolar concentration with Fe2+
-
26% stimulation
-
activation
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1 mM, stimulates
-
40% increase of activity at 2.5 mM
-
0.1 mM, activation
-
1.0 mM, relative activity 108%
-
10 mM, activation to 156% of control
-
50% activation at 10 mM
-
2.4 mM, 1.53fold activation
-
4% increase of activity at 5 mM
-
weak activation
-
enhances activity
-
1-5 mM strongly activates deformylase activity, activity increases 6fold at 1 mM
-
177% activity at 1 mM
-

Inhibitor in Enzyme-catalyzed Reactions (1051 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1.26 mM, 41% inhibition after 1 h, 82% inhibition after 2 h, no change in remaining activity after removal of 1,10-phenanthroline
-
38% inhibition
-
2 mM, 37% inhibition
-
strong inhibition
-
uncompetitive inhibition with respect to NAD+ and competitive inhibition with respect to D-galactose
-
inhibits 96% at 4 mM, reduction reaction
-
at concentrations higher than 3 mM and low concentration of NAD+, about 50% inhibition
-
complete inhibition at 0.1 mM
-
50% inhibition at 0.065 mM
-
70% remaining acitvity at concentration 1 mM
-
weak inhibition
-
50% inhibition at 16.7 mM
-
inhibits 90% at 10 mM
-
slight inhibition at 1 mM
-
wild-type, W86Y and W227Y
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30% of activity at 10 mM
-
54% inhibition at 1 mM, 96% at 5 mM
-
slight inhibition at 1 mM, 50-70% inhibition at 5 mM
-
reduction of aldehyde
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dose dependent decrease in enzyme activity
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1 mM, 71% inhibition
-
1 mM, 30% inhibition
-
inhibition, (R)-2,3-butanediol dehydrogenase activity
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80% inhibition at 5 mM
-
79% inhibition at 1.0 mM, 87% at 10 mM
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10 mM, 15% inhibition
-
10 mM, decrease of 13% in the enzymatic activity
-
0.025 mM, 70% activity lost after 5 min
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50% inhibition at a concentration of 50 mM
-
1 mM, 43% residual activity
-
slight
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5 mM, 87% inhibition
-
88% residual activity at 1 mM
-
IC50: 0.75 mM
-
85% inhibition at 1 mM
-
inhibits competitive Mn(III)-malonate formation
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69% inhibition at 5 mM
-
36% activity at 1 mM
-
45-55% inhibition at 10 mM
-
46% inhibition at 1 mM
-
85% inhibition at 0.1 mM
-
0.005 mM, approx. 50% inhibition after 30 min, complete inhibition after 60 min, complete restoration of inactivated enzyme by addition of excess ferric EDTA complex
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90% inhibition at 0.1 mM
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0.01 mM, 34% inhibition
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inactivation in the absence of O2 due to formation of a white precipitate corresponding to apoprotein
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largely irreversible losses
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Fe2+ chelator, 1 mM, complete inhibition
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2.5 mM, 50% inhibition
-
1 mM, complete loss of activity
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inactivation
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complete inhibition at 1 mM
-
0.01 mM, 89% inhibition
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1 mM, 20% inhibition
-
66.54% residual activity in the presence of 5 mM 1,10-phenanthroline
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slight
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0.1 mM, 35% inhibition
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at 0.02 mM complete inhibition
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complete loss of activity
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2 mM, no residual activity
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10 mM, 63% inhibition of ferredoxinNAP reductase
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100% inhibition at 0.5 mM
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0.5 mM, 82% loss of activity
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1 mM, 34% inhibition
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0.1 mM, 100% inhibition
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2 mM, 40% inhibition. Activity is completely restored by 2 mM Fe2+
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slight inhibition at 0.0005 to 0.001 mM
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chelation of Fe2+
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complete inhibition at 1 mM
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0.05 mM, 70% inhibition
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10% residual activity at 1 mM
-
0.5 mM, 88% inhibition
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44% residual activity at 1 mM
-
47% residual activity at 1 mM
-
83% residual activity at 1 mM
-
weak
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complete inhibition at 0.01 mM
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2.71% residual activity at 0.1 mM
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1 mM, 30-50% inhibition
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5 mM, 33% inhibition
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63% inhibition at 10 mM
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inhibits BZDH by 60%, probably by chelation of tightly bound Mg2+ ions
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1 mM causes 5% inhibition at 30°C
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40% inhibition at 1 mM
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5 mM, 25% inhibition
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0.1 mM, 15% residual activity
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0.1 mM concentration 26% inhibition
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1 mM, inactivates CO/acetyl-CoA exchange activity completely but has no effect on CO oxidation
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50% inhibition at 0.006 mM
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0.025 mM, 50% inhibition. The rate of conversion of violaxanthin to antheraxanthin is relatively unchanged whereas the conversion of antheraxanthin to zeaxanthin is 50-80% inhibited
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1 mM, 10% inhibition
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enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 71% inhibition
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in absence of substrate
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in presence of glutathione
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strong inhibition
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1 mM, 29% inhibition
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5 mM, strong inhibition of isozymes 1-3
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0.05 mM, 50% inhibition
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5 mM, 72% inhibition
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weak inhibition
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17% inhibition at 1 mM
-
0.005 M, 14% inhibition
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0.005 M, 52% inhibition
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1 mM, 78% inhibition
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1 mM, slight inhibition
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53% residual activity at 2 mM
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69% inhibition at 9 mM
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47% inhibition at 2 mM
-
1 mM, 72% inhibition
-
10 mM, 16% inhibition
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1.0 mM
-
1 mM, complete inhibition
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72% inhibition at 2 mM
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slight
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at 1 mM 60% inhibition
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50% inhibition at 0.12 mM
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15% inhibition at 5 mM
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0.1 mM, 56% inhibition
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1 mM, complete inhibition. 1,10-Phenanthroline additionally has inhibitory effects on growth of Peptoclostridium difficile
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weak
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2 mM, 82% inhibition, 1 mM, 73% inhibition
-
slightly inhibitory
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93.1% residual activity after 1 h at 1 mM
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to some extent
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0.1 mM, 30% inhibition
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20% residual activity at 20 mM
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not reversible by Ca2+
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slight inhibition of free and immobilized enzyme
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0.01 mM, 91% inhibition
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causes 50% inhibition
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strong inhibition at 5 mM
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1 mM, 84% residual activity
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14% inhibition at 1 mM
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activity is restored by Fe2+ or Zn2+
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inhibits reactivation of O2-inactivated enzyme
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20 mM, 96% inhibition
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not m-isomer
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inhibition of AMP incorporating activity only, the CMP incorporating activity is much less sensitive
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34% inhibition at 10 mM
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55% remaining activity after 5 min, 18% remaining activity after 60 min, 1 mM
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dose-dependent inhibition
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80% relative residual activity
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19% inhibition by 1 mM, 27% inhibition by 2 mM
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20 mM, strong inhibition
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inhibition of Mn2+-dependent enzyme, no inhibition of the Mg2+-dependent enzyme
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inhibition of cytosolic and membrane-bound enzyme
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0.24 mM, complete inhibition of plasmid nicking activity
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99% inhibition
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0.3 mM, more than 95% inhibition
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slight inhibition at 10 mM
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no inhibition of isozyme MG4, 22.5 inhibition of isozyme MG6
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inhibits the acid trehalase, inhibits the neutral trehalase in presence of 5 mM trehalose; inhibits the neutral trehalase in presence of 5 mM trehalose
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1 mM, 75% inhibition
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less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB1 decreases by 50%; less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB2 decreases by 50%
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concentration of 1 mM causes 25% inhibition
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6 mM, 70% inhibition
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strong inhibitor, after preincubation of the purified enzyme for 1 h at 0°C
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63.3% residual activity at 5 mM
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IFO 3134, slight inhibition
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5 mM, no inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 5% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
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1 mM, 23% inhibition
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27% inhibition at 1 mM
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5 mM, 67% residual activity
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noncompetitive
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1 mM, complete inhibition
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1 mM, 90% inhibition
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100% inhibition at 1 mM
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reactivation by zinc, cobalt and manganese ions
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inhibits at a molar ratio of inhibitor to enzyme of 50:1
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20% inhibition at 0.01 mM, 55% inhibition at 0.1 mM, 64% inhibition at 0.5 mM
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at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 40%
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at 5 mM
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substrates Nalpha-benzoyl-DL-Arg-4-nitroanilide, acetyl-Leu-Leu-Arg-4-nitroanilide, anticompetitive
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zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
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weak
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10% inhibition at 2 mM
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1 mM, 34% inhibition
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15.28% inhibition at 0.1 mM
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complete inhibition at 1 mM
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1 mM, 73% loss of activity
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94.2% inhibition at 0.5 mM, 100% at 5 mM
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complete inhibition at 0.1 mM
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by 2 mM
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inhibits the hemorrhagic and proteolytic activity of HR1A
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total inhibition at 10 mM
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totally inhibits at 4 mM
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1 mM, complete inhibition of aggrecanase 1 and 2
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activity can be restored by Ca2+
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complete inhibition
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inhibition of the soluble isozyme SEP
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complete inhibition at 1 mM
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strong
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4 mM, complete inhibition
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10 mM, 90% inhibition
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hemorrhagic as well as the proteinase activity is inhibited
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1 mM, no residual activity
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0.1 mM, 8.3% inhibition
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0.1 mM, 82% inhibition of the enzyme isolated on the Ni-affinity column. 0.1mM 1,10-phenanthroline produces no signifiant inhibition of the enzyme isolated on the Zn-affinity column and 10% activity remains after treatment with 1 mM 1,10-phenanthroline. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity, but Ca2+ and Mg2+ produce no restoration of activity; inhibition of the Zn enzyme by 1,10-phenanthroline is slower or less complete than inhibition of the Ni enzyme. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity
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the Fe-containing compound inhibits the enzyme activity
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zinc-specific chelator
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2 mM, 90-100% inhibition
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20-30% inhibition at 1 mM
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84% inhibition at 50 mM
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Ki: 1.3 mM
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5 mM, 67% inhibition
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weak
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weak
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o-phenanthroline, 10 mM: 97% inhibition, partially reversed by CuCl2, CoCl2 and to a lesser extent by ZnCl2 and MnCl2, 1 mM: 29% inhibition, 0.1 mM: no inhibition. 2.5 mM: 73% inhibition, totally reversed by 0.66 mM ZnCl2, CuCl2 or CoCl2 and to a lesser extent also by nickel and manganous ions
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10 mM, 18% loss of activity
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strong inhibition
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rapid inactivation even at an alkaline pH, 9.3
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10 mM, 66% inhibition
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25% inhibition at 0.1 mM
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2 mM, 80% inhibition
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inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
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1 mM, 4.7% inhibition
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1 mM, 45% loss of activity. 1 mM, 91% loss of activity
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5 mM abolishes activity up to 70%
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72% inhibition, not due to metal removal
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complete inhibition at 5 mM
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weak, 2-mercaptoethanol partially protects
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inhibits 98% at 1 mM
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5 mM causes near full inactivation in 1.5 h
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2 mM, 66% inhibition
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20% inhibition at 1 mM
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complete inhibition, recovered by the subsequent supplementation with Zn2+
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complete inhibition, reversible by addition of Fe2+, Mn2+, or Co2+
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1 mM, 95% inhibition
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1 mM, 50% inactivation
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10 mM, 4.5% residual activity
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1 mM, 85% inhibition
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the enzyme is completely inhibited by the presence of 2 mM o-phenanthroline
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40% residual activity at 0.1 mM
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16% inhibition at 0.1 mM
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loss of activity within 5 min in the presence of 40 mM pseudouridine synthetase Pus1
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5 mM, 75% residual activity
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relative activity: 95%
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weak, 20% inhibition at 10 mM
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24% loss of activity in the deamination reaction of L-threo-3-methylaspartate
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20 mM, complete inactivation
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2 mM, 20% inhibition
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10 mM, almost complete inhibition
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inhibition after enzyme dialysis against 0.001 M o-phenanthroline
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weak
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ATP protects the enzyme against zinc removal
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-
-
-
-
-
-
-
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inactivation follows pseudo-first-order kinetics, the rate of inactivation is greater at low enzyme concentrations
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complete inhibition of Na+ transport at 0.5 mM
-

Metals and Ions (1 result)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
results in unfolding and loss of catalytic activity at 10 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (81 results)

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EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

Ki Value (29 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.025
-
-
0.75
-
30°C, pH 7.1
0.115
-
-
0.02
-
-
0.0055
-
-
2
-
-
0.00345
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at pH 8.0 and 25°C
0.0003
-
pH 8.0, 22°C
0.12
-
-
0.028
-
-
1.2
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pH 7.8, 37°C
0.05
-
-
0.26
-
-
0.0001
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98% inhibition
1.3
-
-
0.17
-
-
0.0073
-
-

IC50 Value (41 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.18
-
-
0.75
-
IC50: 0.75 mM
0.00139
-
pH not specified in the publication, temperature not specified in the publication
2
-
at pH 7.6 and 30°C
0.07
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pH 7.2, 23°C
0.0293
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IC50: 0.0293 mM
0.2
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in 10 mM 1,3-bis[tris(hydroxymethyl)methylamino]propane, pH 8.0, 100 mM NaCl, at 37°C
0.002
-
IC50 is 0.0020 mM
0.18
-
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0.2
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IC50: 0.2 mM. Inhibitory effect is substantially potentiated by both EDTA and EGTA. A combined and complete inhibition of the enzyme activity by 0.1 mM EDTA and 0.1 mM 1,10-phenanthroline can be prevented in the presence of 0.04-0.1 mM ZnCl2
0.06
-
IC50 is 0.06 mM
0.015
-
pH 7.0, temperature not specified in the publication
0.1
-
-
0.155
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity

References & Links

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Links to other databases for 1,10-phenanthroline

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EXTERNAL LINKS
ChEBI
PubChem
UniChem