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Information on EC 1.3.5.1 - succinate dehydrogenase and Organism(s) Rattus norvegicus and UniProt Accession Q920L2
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1.3.5.1 succinate dehydrogenaseIUBMB Comments
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively. Under aerobic conditions the enzyme catalyses succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II). Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor. The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit. These enzymes catalyse an electrogenic reaction and are thus classified as EC 7.1.1.12, succinate dehydrogenase (electrogenic, proton-motive force generating).
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- 1.3.5.1
- paragangliomas
- fiber
- malate
- atpase
- citrate
-
light-harvesting
-
tricarboxylic
- pheochromocytoma
-
germline
-
histocompatibility
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-
3-nitropropionic
- photosystems
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-
fungicide
-
chlorophyl
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-
krebs
- flavoproteins
-
histochemistry
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-
bioenergetics
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- huntington
- striatal
- gastrocnemius
-
cytochemical
- mtdna
- aconitase
- glucose-6-phosphatase
- antenna
- rotenone
-
gist
- antimycin
-
oxphos
- lateralis
-
vastus
- myofibrillar
-
supercomplexes
-
submitochondrial
- hippel-lindau
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fast-twitch
-
pdgfra
-
subsarcolemmal
- plantaris
-
non-photochemical
-
excitonic
- biotechnology
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- molecular biology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
succinate dehydrogenase, complex ii, succinic dehydrogenase, mitochondrial complex ii, succinate dehydrogenase complex, mitochondrial succinate dehydrogenase, succinate dehydrogenase subunit b, succinate dehydrogenase b, sdhcdab, succinate-ubiquinone oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
complex II
dehydrogenase, succinate
-
-
-
-
Fcc3
-
-
-
-
FL cyt
-
-
-
-
Flavocytochrome c3
-
-
-
-
FRD
-
-
-
-
fumarate reductase
-
-
-
-
fumarate reductase complex
-
-
-
-
fumaric hydrogenase
-
-
-
-
Ifc3
-
-
-
-
Iron(III)-induced flavocytochrome C3
-
-
-
-
menaquinol-fumarate oxidoreductase
-
-
-
-
menaquinol:fumarate oxidoreductase
-
-
-
-
SDH
-
-
succinate dehydrogenase (quinone)
-
-
-
-
succinate dehydrogenase complex
-
-
-
-
succinate oxidoreductase
-
-
-
-
succinate-coenzyme Q reductase
-
-
-
-
succinic acid dehydrogenase
-
-
-
-
succinic dehydrogenase
-
-
-
-
succinodehydrogenase
-
-
-
-
succinyl dehydrogenase
-
-
-
-
additional information
complex II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively. Under aerobic conditions the enzyme catalyses succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II). Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor. The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit. These enzymes catalyse an electrogenic reaction and are thus classified as EC 7.1.1.12, succinate dehydrogenase (electrogenic, proton-motive force generating).
CAS REGISTRY NUMBER
COMMENTARY
9002-02-2
-
9028-11-9
-
9076-99-7
cf EC 1.3.1.6
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
succinate + 1-methoxy-5-methylphenazinium methyl sulfate
fumarate + ?
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
-
-
-
-
?
succinate + ferricyanide
fumarate + ferrocyanide
-
the assay is based on the reduction of ferricyanide to ferrocyanide by SDH activity and on the coupled capture of ferrocyanide by copper. The granular reaction product (copperferrocyanide) is highly electron opaque and is confined exclusively to the mitochondrial membranes.The use of a chelating agent in the incubating medium prevents the diffusion of the dark spots and guarantees their precise localization at the site of SDH activity
-
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
in presence of phenazine methosulfate
-
-
?
additional information
?
-
the flavoprotein of succinate dehydrogenase is an in vitro substrate of and phosphorylated at Tyr535 and Tyr596 by the Fgr tyrosine kinase, overview
-
-
?
additional information
?
-
determination of the activity of succinate dehydrogenase by 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyl-tetrazolium bromide reduction and by reduction of electron acceptor dichlorophenolindophenol (DCPIP)
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
enzyme assay using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide method
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Cd2+
-
inhibits possibly due of interfering with energy transport mechanism
clozapine
-
chronic administration of the antipsychotic agent, inhibit SDH activity only in the striatum
haloperidol
-
chronic administration of the antipsychotic agent, inhibits SDH activity in the hippocampus and striatum but not in the cerebellum, cortex, and prefrontal cortex
olanzapine
-
chronic administration of the antipsychotic agent, inhibits SDH activity only in the cerebellum, but not in the hippocampus, striatum, cortex, and prefrontal cortex
papyriferic acid
-
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
siccanin
-
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
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
-
inhibits the enzyme of skeletal muscle and liver
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
-
inhibits the enzyme of heart, skeletal muscle, liver, and kidney
trans-[RuCl2(3-pyridinecarboxylic acid)4]
-
inhibits the enzyme of hippocampus, cerebral cortex, heart and liver
trans-[RuCl2(4-pyridinecarboxylic acid)4]
-
inhibits the enzyme of heart and hippocampus
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
-
additional information
-
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
-
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aripiprazole
-
chronic administration of the antipsychotic agent, increases SDH activity in the prefrontal cortex at high doses of 20 mg/kg body weight
medium-chain triglycerides ketogenic diet
-
cytochemical investigation of SDH activity in cardiomyocytes of late adult rats fed for 8 weeks with a medium-chain triglycerides ketogenic diet is performed. Young, age-matched and old animals fed with a standard chow are used as controls. It is shown that the medium-chain triglycerides ketogenic diet intake partially recovers age-related decrease of SDH activity and increases the myocardial area occupied by metabolically active mitochondria. These effects might counteract metabolic alterations leading to apoptosis-induced myocardial atrophy and failure during aging
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0007 - 0.0011
-
liver SDH in presence of Cd2+, pH not specified in the publication, temperature not specified in the publication
0.026
-
liver SDH, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
activities in hyperadrenergic newborn or adult rat leukocytes, overview
additional information
-
enzyme activity in motoneurons of soleus and tibialis anterior muscles, overview
additional information
-
mean initial reaction velocities in four areas of lateral pterygoid muscle from rat brain, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
flavoprotein subunit of thr succinate dehydrogenase; gene sdhA
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
significant decrease in activity following aluminium exposure. Post-treatment with centrophenoxine restores the altered enzyme activity
-
significant decrease in activity following aluminium exposure. Post-treatment with centrophenoxine restores the altered enzyme activity
-
from newborn and adult rats both in hyperadrenergic status, the activity in newborn rats is 3-8fold higher than in adult rats
-
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
-
decreased complex II activity in diabetic hearts compared to control
-
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
-
chlorpyrifos intoxication causes significant inhibition in the level of succinate dehydrogenase
-
lateral pterygoid muscle in the head, activity in single muscle fibers in situ, the activity is higher in the upper and lateral areas than in the medial and lower areas, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
391081, 654172, 657158, 673796, 685306, 686054, 688533, 689109, 689159, 689285, 695601, 698668, 712595, 762781
-
the effect of papyriferic acid on the oxidation of succinate by SDH is examined in mitochondrial preparations from livers
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
acetylation can participate in the modulation of the enzymatic activity of SDH, a key enzyme of the tricarboxylic acid cycle, along with the well-known mechanisms of inhibition by oxaloacetic acid, oxidative stress, or mutations in enzyme subunits, in maintaining the energy supply, membrane potential, and other functions of mitochondria
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
metabolism
-
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
physiological function
-
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SDHA_RAT
656
0
71615
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the flavoprotein of succinate dehydrogenase is an in vitro substrate of and phosphorylated at Tyr535 and Tyr596 by the Fgr tyrosine kinase, mass spectrometric analysis, overview
phosphoprotein
-
FGR tyrosine kinase is one of the kinases that target SDHA at positions Y535 and Y596 (of rat sequence). ROS mediates the activation of FGR tyrosine kinase which phosphorylates SDHA at Y604 and that this function of FGR is required for the adjustment of metabolism under various conditions such as nutrient restriction, hypoxia/reoxygenation, and T-cell activation. This regulation together with the function of phagosomal NADPH oxidase (a source of ROS generation) seems to be essential for the activation of anti-bacterial response in macrophages through committing complex I and II (SDH) to respiration rather than their assembly. Additional to FGR, c-Src is another mitochondrial tyrosine kinase which targets both NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr193 of respiratory complex I and SDHA at Tyr215 of complex II. NDUFV2 phosphorylation is required for NADH dehydrogenase activity, which affects both respiration and cellular ATP content. SDHA phosphorylation, on the other hand, does not alter the enzyme activity but disconcerts electron transfer resulting in the generation of reactive oxygen species. The T98G cell line and the primary neurons expressing the mutants at the corresponding Tyr residues loose viability. These observations thus propound that the mitochondrial c-Src modulates oxidative phosphorylation by phosphorylating two respiratory components and that c-Src activity is essential for cell viability. Dephosphorylation of SDHA is exemplified by PTEN-like mitochondrial phosphatase-1 (PTPMT1), an enzyme which dephosphorylates phosphatidylglycerol phosphate (in cardiolipin biogenesis pathway) and SDHA. Inhibition of PTPMT1 leads to enhanced phosphorylation and activation of SDH and consequently lower glucose concentration. Increased SDH activity lowers glucose levels by at least two mechanisms, by inducing glucose uptake and by boosting the rate of glucose utilization. Collectively these results suggest that PTPMT1 is a major coordinator of glucose utilization by mitochondria
additional information
-
posttranslational modifications regulate SDH levels by 4 means: phosphorylation, deacetylation, succinylation and propionylation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from brain mitochondria by anion and cation exchange chromatography followed by heparin affinity chromatography
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kita, K.; Takamiya, S.; Furushima, R.; Ma, Y.C.; Suzuki, H.; Ozawa, T.; Oya, H.
Electron-transfer complexes of Ascaris suum muscle mitochondria. III. Composition and fumarate reductase activity of complex II
Biochim. Biophys. Acta
935
130-140
1988
Ascaris suum, Bos taurus, Rattus norvegicus
Lemos, R.S.; Fernandes, A.S.; Pereira, M.M.; Gomes, C.M.; Teixeira, M.
Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centers and membrane attachment
Biochim. Biophys. Acta
1553
158-170
2002
Ascaris suum, Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Caenorhabditis elegans, Escherichia coli, facultative anaerobic bacterium, Halobacterium salinarum, Ipomoea batatas, Mammalia, Micrococcus luteus, Mycolicibacterium phlei, Shewanella putrefaciens, Rattus norvegicus, Cereibacter sphaeroides, Rhodospirillum rubrum, Strongyloides ratti, Wolinella succinogenes
Clarkson, G.H.D.; King, T.E.; Lindsay, J.G.
Biosynthesis and processing of the large and small subunits of succinate dehydrogenase in cultured mammalian cells
Biochem. J.
244
15-20
1987
Mammalia, Rattus norvegicus, Sus scrofa
Ackrell, B.A.C.; Armstrong, F.A.; Cochran, B.; Sucheta, A.; Yu, T.
Classification of fumarate reductases and succinate dehydrogenases based upon their contrasting behavior in the reduced benzylviologen/fumarate assay
FEBS Lett.
326
92-94
1993
Ascaris suum, Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Mammalia, Rattus norvegicus
Morita, N.; Iizuka, K.; Okita, K.; Oikawa, T.; Yonezawa, K.; Nagai, T.; Tokumitsu, Y.; Murakami, T.; Kitabatake, A.; Kawaguchi, H.
Exposure to pressure stimulus enhances succinate dehydrogenase activity in L6 myoblasts
Am. J. Physiol.
287
E1064-1069
2004
Rattus norvegicus
Miyadera, H.; Shiomi, K.; Ui, H.; Yamaguchi, Y.; Masuma, R.; Tomoda, H.; Miyoshi, H.; Osanai, A.; Kita, K.; Omura, S.
Atpenins, potent and specific inhibitors of mitochondrial complex II (succinate-ubiquinone oxidoreductase)
Proc. Natl. Acad. Sci. USA
100
473-477
2003
Bos taurus, Rattus norvegicus
Lashin, O.M.; Szweda, P.A.; Szweda, L.I.; Romani, A.M.
Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart
Free Radic. Biol. Med.
40
886-896
2006
Rattus norvegicus
Pettenuzzo, L.F.; Ferreira, G.d.a.C.; Schmidt, A.L.; Dutra-Filho, C.S.; Wyse, A.T.; Wajner, M.
Differential inhibitory effects of methylmalonic acid on respiratory chain complex activities in rat tissues
Int. J. Dev. Neurosci.
24
45-52
2006
Rattus norvegicus
Nehru, B.; Bhalla, P.; Garg, A.
Evidence for centrophenoxine as a protective drug in aluminium induced behavioral and biochemical alteration in rat brain
Mol. Cell. Biochem.
290
33-42
2006
Rattus norvegicus
Goel, A.; Dani, V.; Dhawan, D.K.
Chlorpyrifos-induced alterations in the activities of carbohydrate metabolizing enzymes in rat liver: the role of zinc
Toxicol. Lett.
163
235-241
2006
Rattus norvegicus
Khunderyakova, N.V.; Zakharchenko, M.V.; Zakharchenko, A.V.; Kondrashova, M.N.
Hyperactivation of succinate dehydrogenase in lymphocytes of newborn rats
Biochemistry (Moscow)
73
337-341
2008
Rattus norvegicus
Victor, E.G.; Zanette, F.; Aguiar, M.R.; Aguiar, C.S.; Cardoso, D.C.; Cristiano, M.P.; Streck, E.L.; Paula, M.M.
Effect of ruthenium complexes on the activities of succinate dehydrogenase and cytochrome oxidase
Chem. Biol. Interact.
170
59-66
2007
Rattus norvegicus
Salvi, M.; Morrice, N.A.; Brunati, A.M.; Toninello, A.
Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase
FEBS Lett.
581
5579-5585
2007
Rattus norvegicus (Q920L2)
Kiyomoto, B.H.; Tengan, C.H.; Godinho, R.O.
Effects of short-term zidovudine exposure on mitochondrial DNA content and succinate dehydrogenase activity of rat skeletal muscle cells
J. Neurol. Sci.
268
33-39
2008
Rattus norvegicus
Roy, R.R.; Matsumoto, A.; Zhong, H.; Ishihara, A.; Edgerton, V.R.
Rat alpha- and gamma-motoneuron soma size and succinate dehydrogenase activity are independent of neuromuscular activity level
Muscle Nerve
36
234-241
2007
Rattus norvegicus
Streck, E.L.; Rezin, G.T.; Barbosa, L.M.; Assis, L.C.; Grandi, E.; Quevedo, J.
Effect of antipsychotics on succinate dehydrogenase and cytochrome oxidase activities in rat brain
Naunyn Schmiedebergs Arch. Pharmacol.
376
127-133
2007
Rattus norvegicus
Mizutani, M.; Nakae, Y.; Ohno, N.
Quantitative assessment of succinate dehydrogenase activity of rat lateral pterygoid muscle in undecalcified fresh-frozen section
Okajimas Folia Anat. Jpn.
84
19-24
2007
Rattus norvegicus
Balietti, M.; Fattoretti, P.; Giorgetti, B.; Casoli, T.; Di Stefano, G.; Solazzi, M.; Platano, D.; Aicardi, G.; Bertoni-Freddari, C.
A ketogenic diet increases succinic dehydrogenase activity in aging cardiomyocytes
Ann. N. Y. Acad. Sci.
1171
377-384
2009
Rattus norvegicus
Mogi, T.; Kawakami, T.; Arai, H.; Igarashi, Y.; Matsushita, K.; Mori, M.; Shiomi, K.; Omura, S.; Harada, S.; Kita, K.
Siccanin rediscovered as a species-selective succinate dehydrogenase inhibitor
J. Biochem.
146
383-387
2009
Corynebacterium glutamicum, Escherichia coli, Mus musculus, Pseudomonas aeruginosa, Pseudomonas putida, Rattus norvegicus
McLean, S.; Richards, S.M.; Cover, S.L.; Brandon, S.; Davies, N.W.; Bryant, J.P.; Clausen, T.P.
Papyriferic acid, an antifeedant triterpene from birch trees, inhibits succinate dehydrogenase from liver mitochondria
J. Chem. Ecol.
35
1252-1261
2009
Bos taurus, Rattus norvegicus, Oryctolagus sp.
Karthikeyan, J.; Bavani, G.
Effect of cadmium on lactate dehyrogenase isoenzyme, succinate dehydrogenase and Na+-K+-ATPase in liver tissue of rat
J. Environ. Biol.
30
895-898
2009
Rattus norvegicus, Rattus norvegicus Wistar
Moosavi, B.; Zhu, X.; Yang, W.; Yang, G.
Genetic, epigenetic and biochemical regulation of succinate dehydrogenase function
Biol. Chem.
401
319-330
2020
Brassica sp., Caenorhabditis elegans, Thermus thermophilus, Staphylococcus aureus, Mycobacterium tuberculosis, Mus musculus, Neisseria meningitidis, Rattus norvegicus, Escherichia coli (P0AC41 AND P07014), Homo sapiens (P31040 AND P21912 AND Q99643 AND O14521), Saccharomyces cerevisiae (Q00711 AND P21801 AND P33421 AND P37298)
Fedotcheva, N.; Kondrashova, M.; Litvinova, E.; Zakharchenko, M.; Khunderyakova, N.; Beloborodova, N.
Modulation of the activity of succinate dehydrogenase by acetylation with chemicals, drugs, and microbial metabolites
Biophysics
63
743-750
2018
Rattus norvegicus (Q920L2), Rattus norvegicus Wistar (Q920L2)
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