1.3.5.1: succinate dehydrogenase
This is an abbreviated version!
For detailed information about succinate dehydrogenase, go to the full flat file.
Word Map on EC 1.3.5.1
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1.3.5.1
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paragangliomas
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fiber
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malate
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atpase
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citrate
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light-harvesting
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tricarboxylic
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pheochromocytoma
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germline
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histocompatibility
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isocitrate
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glycogen
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3-nitropropionic
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photosystems
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wistar
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lhcii
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fungicide
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chlorophyl
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tca
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triphosphatase
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krebs
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flavoproteins
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histochemistry
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soleus
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bioenergetics
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thylakoids
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huntington
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striatal
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gastrocnemius
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cytochemical
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mtdna
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aconitase
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glucose-6-phosphatase
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antenna
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rotenone
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gist
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antimycin
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oxphos
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lateralis
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vastus
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myofibrillar
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supercomplexes
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submitochondrial
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hippel-lindau
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fast-twitch
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pdgfra
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subsarcolemmal
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plantaris
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non-photochemical
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excitonic
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biotechnology
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medicine
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diagnostics
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molecular biology
- 1.3.5.1
- paragangliomas
- fiber
- malate
- atpase
- citrate
-
light-harvesting
-
tricarboxylic
- pheochromocytoma
-
germline
-
histocompatibility
- isocitrate
- glycogen
-
3-nitropropionic
- photosystems
- wistar
- lhcii
-
fungicide
-
chlorophyl
- tca
- triphosphatase
-
krebs
- flavoproteins
-
histochemistry
- soleus
-
bioenergetics
- thylakoids
- huntington
- striatal
- gastrocnemius
-
cytochemical
- mtdna
- aconitase
- glucose-6-phosphatase
- antenna
- rotenone
-
gist
- antimycin
-
oxphos
- lateralis
-
vastus
- myofibrillar
-
supercomplexes
-
submitochondrial
- hippel-lindau
-
fast-twitch
-
pdgfra
-
subsarcolemmal
- plantaris
-
non-photochemical
-
excitonic
- biotechnology
- medicine
- diagnostics
- molecular biology
Reaction
Synonyms
8-methylmenaquinol:fumarate reductase, AaSdhB, bacterial succinate:quinone oxidoreductase flavoprotein, complex II, Complex II homolog, complex II of the respiratory chain, complex II succinate:ubiquinone oxidoreductase, DCPIP oxidoreductase, dehydrogenase, succinate, dehydrogenase/complex II, EC 1.3.5.4, EC 1.3.99.1, Fcc3, fdrB, FL cyt, Flavocytochrome c3, FRD, FrdA, FRdABCD, FrdC, FRdCAB, FrdD, fumarate reductase, fumarate reductase complex, fumaric hydrogenase, Ifc3, Iron(III)-induced flavocytochrome C3, iron-sulfur subunit of succinate dehydrogenase, menaquinol-1 fumarate reductase, menaquinol-fumarate oxidoreductase, menaquinol:fumarate oxidoreductase, methylmenaquinol:fumarate reductase, MFR, MFR complex, MfrA, MfrB, mitochondrial complex II, mitochondrial succinate dehydrogenase, mitochondrial succinate:ubiquinone oxidoreductase, More, mQFR, MSMEG_0416, MSMEG_0417, MSMEG_0418, MSMEG_0419, MSMEG_0420, MSMEG_1669, MSMEG_1670, MSMEG_1671, MSMEG_1672, non-classical succinate:quinone reductase, QFR, quinol-fumarate reductase, quinol:fumarate reductase, SDG, SDG-1, SDG-2, SDH, SDH1, SDH2, SDH2-1, SDH2-2, SDH3, SDH4, SdhA, sdhABE, SDHB, SdhC, sdhCAB, SdhCDAB, SdhD, SDISP, SQR, succinate dehydrogenase, succinate dehydrogenase (caldariellaquinone), succinate dehydrogenase (quinone), succinate dehydrogenase B, succinate dehydrogenase complex, succinate dehydrogenase flavoprotein subunit Sdh1p, succinate dehydrogenase iron-sulfur protein, succinate dehydrogenase iron-sulphur protein, succinate dehydrogenase subunit B, succinate oxidoreductase, succinate-2,6-dichlorophenolindophenol oxidoreductase, succinate-coenzyme Q reductase, succinate-quinone oxidoreductase, succinate-quinone reductase, succinate-ubiquinone oxidoreductase, succinate:caldariellaquinone oxidoreductase, succinate:menaquinone 7-reductase, succinate:menaquinone oxidoreductase, succinate:menaquinone reductase, succinate:MK reductase, succinate:quinone oxidoreductase, succinate:quinone reductase, succinate:quinone reductases, succinate:ubiquinone oxidoreductase, succinate:ubiquinone reductase, succinic acid dehydrogenase, succinic dehydrogenase, succinodehydrogenase, succinyl dehydrogenase, Tneu_0423
ECTree
1.3.5.1 succinate dehydrogenaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.3.5.1 - succinate dehydrogenase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-n-heptyl-4 hydroxyquinoline N-oxide
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a specific inhibitor, i.e. HQNO, which binds to quinone binding site Qd in SQR
2-n-heptyl-4-hydroxyquinoline
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inhibition of succinate dehydrogenase activity using 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone or 2,6-dichlorophenolindophenol as electron acceptor
2-n-heptyl-4-hydroxyquinoline N-oxide
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inhibitory to the succinate dehydrogenase activity assay using 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone and 2,6-dichloroindophenol as the electron acceptor, not inhibitory to the succinate dehydrogenase activity assay using phenazine methosulfate and 2,6-dichloroindophenol
2-thenoyltrifluoracetone
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EC50 fumarate reductase 0.026 mM, EC50 succinate dehydrogenase 0.028 mM
2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
3-(difluoromethyl)-1-methyl-N-(1-[(2-bromophenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
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compound exhibits good preventive effects against Rhizoctonia solani
3-(difluoromethyl)-1-methyl-N-(1-[(3,5-dimethylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
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noncompetitive inhibition with respect to cytochrome c and 2,6-dichlorophenol indophenol
3-(difluoromethyl)-1-methyl-N-(1-[(3-methylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
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compound exhibits good preventive effects against Rhizoctonia solani
3-nitropropanoate
treatment with 3-nitroproprionate dissipates the membrane potential of wild-type or Sdh1 mutant cells under hypoxia but not that of cells grown aerobically
5,5'-dithiobis(2-nitro-benzoic acid)
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inactivates, conformation-change type inhibition, the presence of the substrate provides marked protection
5-Hydroxy-2-methyl-1,4-naphthoquinone
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inhibition is only 50% even at 0.1 mM
alpha-tocopheryl succinate
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binds to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
amicarthiazol
i.e. 2-amino-4-methylthiazole -5-carboxanilide, a systemic fungicide. The wild-type enzyme is strongly inhibited by amicarthiazol, while that in resistant mutants is insensitive. A single amino acid substitution H229Y in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, molecular resistance mechanism, overview; i.e. 2-amino-4-methylthiazole-5-carboxanilide, a systemic fungicide. The wild-type enzyme is strongly inhibited by amicarthiazol, while that in resistant mutants is insensitive. A single amino acid substitution H229Y in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, molecular resistance mechanism, overview
antimycin A
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site of inhibition is located at the oxidation side of cytochrome b
Cd2+
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inhibits possibly due of interfering with energy transport mechanism
clozapine
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chronic administration of the antipsychotic agent, inhibit SDH activity only in the striatum
haloperidol
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chronic administration of the antipsychotic agent, inhibits SDH activity in the hippocampus and striatum but not in the cerebellum, cortex, and prefrontal cortex
menaquinone-1
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competitive inhibitor of the succinate oxidation reaction of succinate dehydrogenase
N-[2-(2,4-dichlorophenoxy)phenyl]-3-(difluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
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compound additionally displays good protection effect against Rhizoctonia solani
N-[2-(2-chloro-4-trifluoromethylphenoxy)phenyl]-3-(2-fluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
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noncompetitive with respect to 2,6-dichlorophenol indophenol. Compound additionally displays good protection effect against Rhizoctonia solani
olanzapine
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chronic administration of the antipsychotic agent, inhibits SDH activity only in the cerebellum, but not in the hippocampus, striatum, cortex, and prefrontal cortex
p-benzoquinone
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inhibition of succinate dehydrogenase activity using phenazone methosulfate or 2,6-dichlorophenolindophenol as electron acceptor; inhibitory to the succinate dehydrogenase activity assay using phenazine methosulfate and 2,6-dichloroindophenol
phenylacetate
unlike N-acetylimidazole and acetylsalicylic acid, phenylacetate is not a donor of acetyl groups. It can be assumed that its effect on SDH may be due to both the activation of acetylation and direct interaction with the enzyme
sodium fumarate
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EC50 fumarate reductase 0.6 mM and EC50 succinate dehydrogenase 4.8 mM
sodium malonate
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EC50 fumarate reductase 19 mM and EC50 succinate dehydrogenase 0.68 mM
tetrachlorobenzoquinone
strong inhibition of succinate-phenazine methosulfate-(1,4-dichloroindophenol) oxidoreductase
thiabendazole
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EC50 fumarate reductase 0.46 mM and EC50 succinate dehydrogenase 1 mM
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
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inhibits the enzyme of skeletal muscle and liver
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
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inhibits the enzyme of heart, skeletal muscle, liver, and kidney
trans-[RuCl2(3-pyridinecarboxylic acid)4]
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inhibits the enzyme of hippocampus, cerebral cortex, heart and liver
trans-[RuCl2(4-pyridinecarboxylic acid)4]
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inhibits the enzyme of heart and hippocampus
ubiquinol-2
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competitive inhibitor of the fumarate reduction reaction of fumarate reductase
vitamin E analogues
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epitomised by alpha-tocopheryl succinate affect the electron flow from complex II
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(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
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(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
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1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
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1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
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1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
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1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
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2-(n-heptyl)-4-hydroxy-quinoline N-oxide
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potent inhibitor that affects both reduction and oxidation of quinone, the inhibitor binds close to heme bD
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
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potent inhibitor of fumarate reductase, not inhibitory for succinate dehydrogenase
2-alkyl-4,6-dinitrophenols
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derivatives of 2-alkyl-4,6-dinitrophenols, competitive inhibitors of both succinate dehydrogenase and fumarate reductase
2-alkyl-4,6-dinitrophenols
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complete inhibition of the wild-type enzyme and of the mutants H106Y and H113Q
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
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2-heptyl-4-hydroxyquinoline N-oxide
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
2-n-heptyl-4-hydroxyquinoline-N-oxide
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site of inhibition is located at the oxidation side of cytochrome b
2-Thenoyltrifluoroacetone
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15% inhibition of succinate dehydrogenase activity of larval and adult complex II at 0.1 mM
2-Thenoyltrifluoroacetone
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slows down the inactivation of the enzyme in the substrate assay mixture
2-Thenoyltrifluoroacetone
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inhibits both wild-type and carboxin-resistant enzymes, competitive inhibition with respect to quinone
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
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3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
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3-nitropropionic acid
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irreversible inactivation, 0.00001 mM, 50% inhibition
3-nitropropionic acid
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this study compares the effects of 3-nitropropionic acid in young and old mice. Treatment with 3-nitropropionic acid induces OD in young mice. Old mice present an increase in the basal level of orofacial movement that is not potentiated by any dose of 3-nitropropionic acid. Histochemical analyses show that old mice present an increase in the SDH activity. 3-Nitropropionic acid induces a decrease in SDH activity at both ages
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
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3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
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3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
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3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
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4-Chloromercuriphenyl sulfonate
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inhibitor of the succinate-ubiquinone reductase reaction
4-Chloromercuriphenyl sulfonate
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inhibits the succinate oxidation by cell-derived particles
4-Chloromercuriphenylsulfonate
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inhibits the oxidation of reduced menaquinone by fumarate. Fumarate reductase, measured with reduced benzylviologen as the donor, is not affected
5,5'-dithiobis(2-nitrobenzoate)
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inhibition is reversed by addition of dithiothreitol or dithionite
carboxin
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15% inhibition of succinate dehydrogenase activity of larval and adult complex II at 0.001 mM
carboxin
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Q2-mediated Wurster's blue reduction: 90% inhibition at 0.02 mM, Q0-mediated Wurster's blue reduction: 75% inhibition at 0.02 mM, Q1-mediated Wurster's blue reduction: 88% inhibition at 0.02 mM, Q6-mediated Wurster's blue reduction: 50% inhibition at 0.02 mM
carboxin
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15% inhibition of the succinate-ubiquinone reductase and of the quinol-fumarate reductase reaction, competitive inhibition with quinone or quinol
carboxin
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inhibits the succinate dehydrogenase in the forward and reverse reaction
carboxin
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more than 90% inhibition in isolated membranes at high concentrations, the mutant enzyme is less sensitive than wild-type enzyme
carboxin
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interferes with electron transfer from the 3Fe-4S center to quinone, carboxin may bind to a quinone-binding site the Qp site, close to the 3Fe-4S center, amino acids involved in binding carboxin: a histidine residue in the B subunit and an aspartate residue in the D subunit
nonyl-4-hydroxyquinoline-N-oxide
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the semiquinone analog and inhibitor of quinone reactions in complex II shows no influence on the redox behavior of the heme b moieties
oxaloacetate
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at 0.0006 mM: 20% inhibition of the succinate-ubiquinone reductase reaction and no inhibition of the fumarate reductase reaction, at 0.006 mM: 80% inhibition of fumarate reductase reaction
oxaloacetate
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reactivation by reduction of enzyme with succinate; reactivation with anions
oxaloacetate
the interaction between SDH and oxaloacetate renders the enzyme inactive, while the interaction between the activator and enzyme prevent such interaction with oxaloacetate
papyriferic acid
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papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
papyriferic acid
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papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
papyriferic acid
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papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
Pentachlorophenol
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competitive inhibitor of both succinate dehydrogenase and fumarate reductase
siccanin
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residual activity: 7%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
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residual activity: 13%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
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residual activity: above 1%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
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residual activity: 19%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
thenoyltrifluoroacetate
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inhibits a later step of the electron flow as it binds to the ubiquinone docking sites and abrogates the transfer of electrons to this molecule. It causes a time- and dose-dependent increase of apoptosis. 20% inhibition at 0.5 mM
additional information
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transition from darkness to light causes a short transient increase in the SDH activity followed by a decrease to a half of the original activity
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additional information
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not inhibitory: thenoyltrifluoroacetone, 2-n-heptyl-4-hydroxyquinoline N-oxide
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additional information
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not inhibitory: heptyl 4-hydroxyquinoline N-oxide
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additional information
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residual activity: 97%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
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additional information
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residual activity: above 77%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
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additional information
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different pro-apoptotic agents responsible for complex II inhibition lead to mitochondrial matrix acidification
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additional information
direct effectors are either deactivators such as oxaloacetate or activators such as substrates, anions, reduced quinone, ATP, and reduction
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additional information
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15-20% inhibition of complex II activity in striatum and hippocampus by methylmalonic acid at low concentrations of sucinate in the medium, but not in the peripheral tissue. the inhibitory property only occurs after exposing brain homogenates for at least 10 min with the acid, suggesting that this inhibition is mediated by indirect mechanisms
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additional information
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zidovudine, i.e. 3'-azido-3'-deoxythymidine or AZT, represses the enzyme content in mitochondria of cultured rat muscle cells by 13% via reducing the mitochondrial DNA content by 66% at 0.1 mg/ml, histochemic analysis, overview
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additional information
inhibitory effects of acetylating and deacetylating compounds on the activity of succinate dehydrogenase, as well as effects on the membrane potential and calcium retention capacity of the isolated liver mitochondria, and determination of the possible sites of the enzyme inhibition by the acetylating compounds, overview. Acetylsalicylic acid is the most effective inhibitor of SDH. The inhibition of the enzyme is due to the acetylation of the site binding alpha-ketoglutarate, and it is partially eliminated or prevented by pre-incubation of the mitochondria with nicotinamide adenine dinucleotide, a cofactor for deacetylation, and with polyamine spermidine, an acceptor of acetyl groups. Malonate and thenoyltrifluoroacetate (TTFA), which are specific inhibitors of SDH, as well as the intermediate carrier of electrons phenazine methosulfate (PMS), are used to identify the possible sites of action of these compounds. The influence of NAD, as a cofactor in deacetylation, and polyamine spermidine, as a possible activator of deacetylation, on the modulation of the activity of SDH by acetylating compounds is investigated. PMS prevents the inhibition of SDH caused by TTFA and has no effect on the inhibition induced by malonate. PMS almost completely prevents the inhibition induced by the tested compounds, as does NAD
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