Protein Information

Name succinate dehydrogenase (protein family or complex)
Synonyms Succinate dehydrogenase; Succinate dehydrogenases

Compound Information

Name rotenone
CAS

Reference List

PubMed Abstract RScore(About this table)
4309122 Shephard EH, Hubscher G: Phosphatidate biosynthesis in mitochondrial subfractions of rat liver. . Int J Parasitol. 1995 Feb;25(2):261-3.

Phosphatidate formation was measured in all subcellular fractions and subfractions and was compared with the distribution of succinate dehydrogenase, monoamine oxidase, rotenone-insensitive NADH cytochrome c reductase, arylsulphatase, urate oxidase, arylesterase and glucose 6-phosphatase. 3.
6(0,0,1,1) Details
182253 Hostetler KY, Zenner BD, Morris HP: Abnormal membrane phospholipid content in subcellular fractions from the Morris 7777 hepatoma. J Pharm Pharmacol. 1977 Nov;29(11):657-63.

Mitochondrial and microsomal fractions were prepared from normal rat liver and the Morris 7777 hepatoma and characterized by the use of the marker enzymes, succinate dehydrogenase and rotenone-insensitive NADPH-cytochrome c reductase. 2.
6(0,0,1,1) Details
18615133 Bonsi P, Cuomo D, Martella G, Sciamanna G, Tolu M, Calabresi P, Bernardi G, Pisani A: Mitochondrial toxins in Basal Ganglia disorders: from animal models to therapeutic strategies. Curr Neuropharmacol. 2006 Jan;4(1):69-75.

MPTP and rotenone, both selective inhibitors of mitochondrial complex I have been extensively used to mimic PD.
Conversely, in HD a selective impairment of mitochondrial succinate dehydrogenase, key enzyme in complex II activity was found in medium spiny neurons of the caudate-putamen.
1(0,0,0,1) Details
8383431 Cogswell AM, Stevens RJ, Hood DA: Properties of skeletal muscle mitochondria isolated from subsarcolemmal and intermyofibrillar regions. Am J Physiol. 1993 Feb;264(2 Pt 1):C383-9.

Site 1 inhibition of respiration with rotenone reduced this difference to 1.4-fold.
The activities of cytochrome-c oxidase (CYTOX) and succinate dehydrogenase (SDH) could account for some of these differences, since CYTOX was 20% greater (P < 0.05) in IMF mitochondria, and SDH was 40% greater (P < 0.05) in SS mitochondria.
1(0,0,0,1) Details
2457393 Kottke M, Adam V, Riesinger I, Bremm G, Bosch W, Brdiczka D, Sandri G, Panfili E: Mitochondrial boundary membrane contact sites in brain: points of hexokinase and creatine kinase location, and control of Ca2+ transport. Biochim Biophys Acta. 1988 Aug 17;935(1):87-102.

The fraction was composed of inner and outer limiting membrane components as shown by the specific marker enzymes, succinate dehydrogenase and NADH-cytochrome-c-oxidase (rotenone insensitive).
6(0,0,1,1) Details
8214593 Munujos P, Coll-Canti J, Gonzalez-Sastre F, Gella FJ: Assay of succinate dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron acceptor. Anal Biochem. 1993 Aug 1;212(2):506-9.

2(0,0,0,2) Details
224923 Bers DM: Isolation and characterization of cardiac sarcolemma. Biochim Biophys Acta. 1979 Jul 19;555(1):131-46.

There was very little contamination of the sarcolemmal fraction by sarcoplasmic reticulum (as judged by Ca2+-ATPase and glucose-6-phosphatase activities) or inner mitochondrial membranes (as judged by succinate dehydrogenase activity).
There may, however, be some contamination by outer mitochondrial membranes (as judged by monoamine oxidase and rotenone-insensitive NADH cytochrome c reductase activities) which have rarely been monitored in cardiac sarcolemmal preparations.
1(0,0,0,1) Details
3223930 Raj RK, Puranam RS, Kurup CK, Ramasarma T: Oxidative activities in mitochondria-like particles from Setaria digitata, a filarial parasite. Biochem J. 1988 Dec 1;256(2):559-64.

These worms showed active wriggling movements which were not affected by respiratory poisons such as cyanide, rotenone and malonate.
By differential centrifugation of sucrose homogenates, a fraction containing mitochondria-like particles was obtained in which the activity of the marker enzyme, succinate dehydrogenase, was recovered.
1(0,0,0,1) Details
7622334 Armson A, Grubb WB, Mendis AH: The effect of electron transport (ET) inhibitors and thiabendazole on the fumarate reductase (FR) and succinate dehydrogenase (SDH) of Strongyloides ratti infective (L3) larvae. Toxicol Appl Pharmacol. 1994 Apr;125(2):309-21.

Rotenone (a specific inhibitor of electron transport Complex I) inhibited the S. ratti FR (EC50 = 3.0 x 10 (-7) M) but not SDH.
2(0,0,0,2) Details
2001241 Rustin P, Lance C: Succinate-driven reverse electron transport in the respiratory chain of plant mitochondria. Comp Biochem Physiol B Biochem Mol Biol. 1999 May;123(1):59-65.

The effects of rotenone and adenylates in relation to malate and oxaloacetate metabolism..
At pH 7.9, the oxaloacetate produced progressively inhibited the succinate dehydrogenase.
2(0,0,0,2) Details
8078526 Beattie DS, Obungu VH, Kiaira JK: Oxidation of NADH by a rotenone and antimycin-sensitive pathway in the mitochondrion of procyclic Trypanosoma brucei brucei. Mol Biochem Parasitol. 1994 Mar;64(1):87-94.

The presence of an alternative pathway for NADH oxidation involving fumarate reductase was indicated by the observation that malonate, the specific inhibitor of succinate dehydrogenase, inhibited 30-35% the rate of oxygen uptake with malate and glucose as substrates in the digitonin-permeabilized cells.
1(0,0,0,1) Details
172130 Wagner T, Rafael J: ATPase complex and oxidative phosphorylation in chloramphenicol-induced megamitochondria from mouse liver. J Neurochem. 2000 Dec;75(6):2611-21.


On the other hand succinate dehydrogenase activity is increased by 50%. 6.
1(0,0,0,1) Details
19540189 Moser MD, Matsuzaki S, Humphries KM: Inhibition of succinate-linked respiration and complex II activity by hydrogen peroxide. Arch Biochem Biophys. 2009 Aug 1;488(1):69-75. Epub 2009 Jun 18.

Previous studies, however, have suggested that complex II (succinate dehydrogenase) is sensitive to H (2) O (2)-mediated inhibition.
It was found that conditions which prevent oxaloacetate accumulation during state 3 respiration, such as inclusion of rotenone, glutamate, or ATP, blunted the effect of H (2) O (2) on succinate-linked respiration and complex II activity.
1(0,0,0,1) Details
8841128 Panov A, Scarpa A: Mg2+ control of respiration in isolated rat liver mitochondria. . Biochemistry. 1996 Oct 1;35(39):12849-56.


In contrast, similar cation depletion stimulates succinate dehydrogenase (or glutamate dehydrogenase) in state 4 without decreasing membrane potential.
1(0,0,0,1) Details
1898100 Glinn M, Ernster L, Lee CP: Initiation of lipid peroxidation in submitochondrial particles: effect of respiratory inhibitors. Arch Biochem Biophys. 1991 Oct;290(1):57-65.

The two nicotinamide nucleotides exhibited different activities in initiating lipid peroxidation with regard to concentration and to the effects of rotenone and rhein.
Lipid peroxidation is thought to be enzymatically induced in both the NADH and the succinate dehydrogenase regions of the respiratory chain, and evidence is presented for a novel pathway of NADPH oxidation that may also be involved.
1(0,0,0,1) Details
1329742 Huertas R, Campos Y, Diaz E, Esteban J, Vechietti L, Montanari G, D'Iddio S, Corsi M, Arenas J: Respiratory chain enzymes in muscle of endurance athletes: effect of L-carnitine. Biochem Biophys Res Commun. 1992 Oct 15;188(1):102-7.

Athletes receiving L-carnitine showed a significant increase (p < 0.01) in the activities of rotenone-sensitive NADH cytochrome c reductase, succinate cytochrome c reductase and cytochrome oxidase.
In contrast, succinate dehydrogenase and citrate synthase were unchanged.
1(0,0,0,1) Details
8171438 Medrano CJ, Fox DA: Substrate-dependent effects of calcium on rat retinal mitochondrial respiration: physiological and toxicological studies. J Dairy Sci. 1975 Sep;58(9):1282-7.

Isolated mitochondria were efficiently coupled; had good respiratory control ratios with the NAD-linked substrates, glutamate or pyruvate plus malate (G/M or P/M), and the FAD-linked substrate, succinate plus rotenone (S/R); and possessed a Na+/Ca2+ exchanger.
Results with G/M suggest that Ca2+ acts on the inner membrane phospholipase A2 to decrease NADH CoQ reductase activity and/or produce a NAD+ leak, whereas with S/R, Ca2+ may inhibit succinate dehydrogenase.
1(0,0,0,1) Details
7678739 Hennet T, Richter C, Peterhans E: Tumour necrosis factor-alpha induces superoxide anion generation in mitochondria of L929 cells. Biochem J. 1993 Jan 15;289 ( Pt 2):587-92.

The generation of superoxide anion (O2.-) was sensitive to treatment with rotenone, antimycin A and cyanide, indicating that the signal originated from mitochondria.
In addition, we detected a decreased activity of the mitochondrial enzyme succinate dehydrogenase in these cells, suggesting that this component of the respiratory chain might be an important contributor to the TNF alpha-induced generation of O2.-.
1(0,0,0,1) Details
10378416 Chen M, Andersen LP, Zhai L, Kharazmi A: Characterization of the respiratory chain of Helicobacter pylori. FEMS Immunol Med Microbiol. 1999 Jun;24(2):169-74.

The total insensitivity of activities of NADH dehydrogenase to rotenone and of NADH-cytochrome c reductase to antimycin is indicative of the absence of the classical complex I of the electron transfer chain in this bacterium.
Fumarate and malonate exhibited a concentration-dependent inhibitory effect on the activity of succinate dehydrogenase.
1(0,0,0,1) Details
2174736 Modica-Napolitano JS, Joyal JL, Ara G, Oseroff AR, Aprille JR: Mitochondrial toxicity of cationic photosensitizers for photochemotherapy. Cancer Res. 1990 Dec 15;50(24):7876-81.


With photoirradiation VB-BO was also shown to inhibit rotenone-sensitive NADH-cytochrome c reductase activity, but it had no effect on succinate-cytochrome c reductase activity.
0(0,0,0,0) Details
7994564 Chen CL, Sangiah S, Yu CA, Chen H, Berlin KD, Garrison GL, Scherlag BJ, Lazzara R: Effects of novel antiarrhythmic agents, BRB-I-28 and its derivatives, on the heart mitochondrial respiratory chain and sarcoplasmic reticulum Ca (2+)-ATPase. Res Commun Mol Pathol Pharmacol. 1994 Aug;85(2):193-208.


The site of inhibition of BRB-I-28 and its derivatives on the respiratory chain was localized between flavoprotein n (FPn) and CoQ, which is similar to the effect of rotenone and several other antiarrhythmic drugs such as amiodarone, propranolol, etc.
0(0,0,0,0) Details
11080215 Talpade DJ, Greene JG, Higgins DS Jr, Greenamyre JT: In vivo labeling of mitochondrial complex I (NADH:ubiquinone oxidoreductase) in rat brain using [(3) H] dihydrorotenone. Biochem J. 1991 Feb 15;274 ( Pt 1):249-55.

In vivo [(3) H] DHR binding was markedly reduced by local and systemic infusion of rotenone and was enhanced by local NADH administration.
There was an excellent correlation between regional levels of in vivo [(3) H] DHR binding and the in vitro activities of complex II (succinate dehydrogenase) and complex IV (cytochrome oxidase), suggesting that the stoichiometry of these components of the electron transport chain is relatively constant across brain regions.
1(0,0,0,1) Details
19526285 Mallajosyula JK, Chinta SJ, Rajagopalan S, Nicholls DG, Andersen JK: Metabolic control analysis in a cellular model of elevated MAO-B: relevance to Parkinson's disease. Neurotox Res. 2009 Oct;16(3):186-93. Epub 2009 Mar 5.


In addition to KGDH, we assessed the activities and substrate-mediated respiration of complex I, pyruvate dehydrogenase (PDH), succinate dehydrogenase (SDH), and mitochondrial aconitase in the absence and presence of complex-specific inhibitors in specific and mixed substrate conditions in mitochondria from our MAO-B elevated cells versus controls.
1(0,0,0,1) Details
12241070 Mildaziene V, Nauciene Z, Krab K: The targets of 2,2',5,5'-tetrachlorobiphenyl in the respiratory chain of rat liver mitochondria revealed by modular kinetic analysis. Mol Biol Rep. 2002;29(1-2):31-4.


The effects of 20 microM 2,2',5,5'-TCB on the activity of the respiratory chain modules in rat liver mitochondria oxidizing succinate (+ rotenone) in state 3 were assessed.
0(0,0,0,0) Details
12781335 Lembert N, Idahl LA, Ammon HP: K-ATP channel independent effects of pinacidil on ATP production in isolated cardiomyocyte or pancreatic beta-cell mitochondria. Biochem Pharmacol. 2003 Jun 1;65(11):1835-41.

This PIN-dependent stimulation was mimicked by rotenone.
In cardiomyocytes with metabolically inhibited succinate dehydrogenase this results in a stimulation of ATP production conferring tissue protection.
1(0,0,0,1) Details
3813563 Kucera I, Kozak L, Dadak V: Is the ubiquinone pool in the respiratory chain of the bacterium Paracoccus denitrificans really unhomogeneous?. Arch Biochem Biophys. 1987 Feb 15;253(1):199-204.


The deviation from the expected behavior observed in comparing the titration of NADH oxidase and succinate oxidase with respiratory inhibitors such as mucidin (inhibitor in the bc1 region) or cyanide can be accounted for by the activation of succinate dehydrogenase upon the increase in the reduced state of respiratory components during the titration.
1(0,0,0,1) Details
6269601 Schewe T, Albracht SP, Ludwig P: On the site of action of the inhibition of the mitochondrial respiratory chain by lipoxygenase. Biochim Biophys Acta. 1981 Jul;636(2):210-7.

The inhibitory blockage is located between both the NADH and succinate dehydrogenases and Q-10.
The Fe-S clusters of the mitochondrial outer membrane are destroyed by lipoxygenase treatment, without any effect on the rotenone-insensitive NADH: cytochrome c oxidoreductase activity.
1(0,0,0,1) Details
612129 Kassabova T, Russanov E: Effect of chronic copper loading on the functions of rat liver mitochondria. Acta Physiol Pharmacol Bulg. 1977;3(3):42-8.


H-DCPIP-reductase, succinate-cytochrome c (DCPIP)-reductase and succinate dehydrogenase) depending on the duration of copper sulphate treatment and hepatic copper level.
1(0,0,0,1) Details
10888471 Rustenbeck I, Dickel C, Herrmann C, Grimmsmann T: Mitochondria present in excised patches from pancreatic B-cells may form microcompartments with ATP-dependent potassium channels. Biosci Rep. 1999 Apr;19(2):89-98.

Likewise, the inhibitor of succinate dehydrogenase, malonate (5 mM), increased the open probability of K (ATP) channels in the presence of succinate (1 mM).
However, oligomycin in combination with antimycin and rotenone did not increase open probability.
1(0,0,0,1) Details
5160697 Nelson BD, Norling B, Persson B, Ernster L: Effect of thenoyltrifluoroacetone on the interaction of succinate dehydrogenase and cytochrome b in ubiquinone-depleted submitochondrial particles. Biochem Biophys Res Commun. 1971 Sep 17;44(6):1312-20.

1(0,0,0,1) Details
12411515 Hanley PJ, Ray J, Brandt U, Daut J: Halothane, isoflurane and sevoflurane inhibit NADH:ubiquinone oxidoreductase (complex I) of cardiac mitochondria. Biochem J. 1969 Jun;113(2):429-40.

In addition to inhibiting NADH oxidation, halothane also inhibited succinate oxidation (and succinate dehydrogenase), albeit to a lesser extent.
Unlike the classical inhibitor rotenone, none of the anaesthetics completely inhibited enzyme activity at high concentration, suggesting that these agents bind weakly to the 'hydrophobic inhibitory site' of complex I.
1(0,0,0,1) Details
17332268 Menshikova EV, Ritov VB, Ferrell RE, Azuma K, Goodpaster BH, Kelley DE: Characteristics of skeletal muscle mitochondrial biogenesis induced by moderate-intensity exercise and weight loss in obesity. J Appl Physiol. 2007 Jul;103(1):21-7. Epub 2007 Mar 1.

Enzyme activity of the ETC increased (P < 0.01); that for rotenone-sensitive NADH-oxidase (96 +/- 1%) increased more than for ubiquinol-oxidase (48 +/- 6%).
Activities for citrate synthase and succinate dehydrogenase increased by 29 +/- 9% and 40 +/- 6%, respectively.
1(0,0,0,1) Details
1176438 Hillar M, Lott V, Lennox B: Correlation of the effects of citric acid cycle metabolites on succinate oxidation by rat liver mitochondria and submitochondrial particles. J Bioenerg. 1975 Mar;7(1):1-16.

Succinate dehydrogenase is inhibited by citrate and beta-hydroxy-butyrate in a complex manner, both in mitochondria and submitochondrial particles.
Stimulation by alpha-ketoglutarate and glutamate is not influenced by the presence of rotenone. 4.
1(0,0,0,1) Details
7727510 Gonzalez-Flecha B, Boveris A: Mitochondrial sites of hydrogen peroxide production in reperfused rat kidney cortex. Biochim Biophys Acta. 1995 Apr 13;1243(3):361-6.

H2O2 production rates were assessed in isolated mitochondria using either succinate, with and without antimycin, or malate-glutamate, with and without rotenone.
Respiratory activities of isolated mitochondria and activity of NADH- and succinate-cytochrome c reductase and of NADH- and succinate-dehydrogenase in submitochondrial particles were measured to evaluate the electron flux throughout respiratory carriers.
1(0,0,0,1) Details
9932647 Sreeramulu K, Schmidt CL, Schafer G, Anemuller S: Studies of the electron transport chain of the euryarcheon Halobacterium salinarum: indications for a type II NADH dehydrogenase and a complex III analog. J Bioenerg Biomembr. 1998 Oct;30(5):443-53.

These activities could be blocked by the following inhibitors: 7-jodocarboxylic acid, giving evidence for the presence of a type II NADH dehydrogenase, antimycin A, and myxothiazol, indicating the presence of a complex III analog, and the typical succinate dehydrogenase (SDH) and terminal oxidase inhibitors.
Complex I inhibitors like rotenone and annonine were inactive, clearly excluding the presence of a coupled NADH dehydrogenase.
1(0,0,0,1) Details
6245637 Ingledew WJ, Ohnishi T: An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria. Biochem J. 1980 Jan 15;186(1):111-7.

The apparent midpoint potentials of Centre N-2 (NADH dehydrogenase) and S-1 (succinate dehydrogenase) and their pH-dependence was also determined by using the succinate/fumarate couple.
Oxidation-reduction titrations of iron-sulphur centres with the couple NADH/NAD+ and an analogue APADH/APAD+ in the presence of rotenone gave results substantially different from those obtained by redox potentiometry; these differences may be due to the mechanism of action of NADH dehydrogenase and its specific interaction with NADH. 5.
1(0,0,0,1) Details
10425713 Obungu VH, Kiaira JK, Njogu RM, Olembo NK: Catabolism of proline by procyclic culture forms of Trypanosoma congolense. 131-40.

Rotenone had no effect on the rate of respiration except when the intact cells were first permeabilized by digitonin after which rotenone decreased the rate of respiration by 20-30%.
Enzymes involved in the catabolism of proline with high activities were: proline dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, fumarase, NADP-linked malic enzyme, alanine aminotransferase and malate dehydrogenase.
1(0,0,0,1) Details
171290 Baumrucker CR, Keenan TW: Membranes of mammary gland. Biochem Pharmacol. 1997 Feb 7;53(3):299-308.

These marker enzymes include: Succinate dehydrogenase (mitochondria), nicotinamide adenine dinucleotide phosphate cytochrome c reductase and, to a lesser extent, retenone insensitive nicotinamide adenine dinucleotide cytochrome c reductase (endoplasmic reticulum), galactosyl transferase (Golgi apparatus), 5'-nucleotidase (plasma membranes), uric acid oxidase (microbodies), and acid phosphatase (lysosomes).
Rotenone sensitive nicotinamide adenine dinucleotide cytochrome c reductase and sodium, potassium, magnesium-stimulated adenosine triphosphatase were widely distributed among subcellular fractions and are not valid marker enzymes.
1(0,0,0,1) Details
444501 Le Quoc K, Le Quoc D, Gaudemer Y: Influence of the energetic state of mitochondria on the inhibition of oxidative phosphorylation by N-ethylmaleimide. Biochim Biophys Acta. 1979 May 9;546(2):356-64.

N-Ethylmaleimide inhibitory effect on oxidative phosphorylation, adenylic nucleotide translocation, succinate dehydrogenase and succinoxidase activities was studied as a function of the energetic state of mitochondria. 1.
Using a reversible thiol reagent (mersalyl), in order to protect the phosphate carrier against irreversible action of N-ethylmaleimide, it was found that: (a) when mersalyl-pretreated mitochondria were in a 'non-energized' state, i.e. preincubated without a substrate and in the presence of rotenone, only a slight inhibition of succinate oxidation coupled to ATP synthesis by N-ethylmaleimide was observed. (b) when mersalyl-pretreated mitochondria were in an 'energized' state, i.e. preincubated in the presence of an oxidizable substrate, N-ethylmaleimide strongly inhibited the coupled oxidation of succinate. 2.
1(0,0,0,1) Details
3514901 Ginsburg H, Divo AA, Geary TG, Boland MT, Jensen JB: Effects of mitochondrial inhibitors on intraerythrocytic Plasmodium falciparum in in vitro cultures. J Protozool. 1986 Feb;33(1):121-5.


In the present study, inhibitors of mitochondrial function including compounds which act on NADH and succinate dehydrogenases, electron transport and mitochondrial ATPase, as well as uncouplers, were found to inhibit the growth and propagation of the human parasite Plasmodium falciparum in in vitro cultures at concentrations that specifically affect mitochondrial functions.
1(0,0,0,1) Details
15151993 Gauthier BR, Brun T, Sarret EJ, Ishihara H, Schaad O, Descombes P, Wollheim CB: Oligonucleotide microarray analysis reveals PDX1 as an essential regulator of mitochondrial metabolism in rat islets. J Biol Chem. 2004 Jul 23;279(30):31121-30. Epub 2004 May 19.

Rotenone, an inhibitor of complex I, mimicked this effect.
Quantitative reverse transcriptase-PCR confirmed increases in succinate dehydrogenase and ATP synthase mRNAs as well as pyruvate carboxylase and the transcript for the malate shuttle.
1(0,0,0,1) Details
1804136 Anokhina IP, Gorkin VZ, Medvedev AE, Ovchinnikova LN, Khristolyubova NA: Studies on mitochondrial metabolic processes in offspring of alcoholized rats--I. Alcohol Alcohol. 1991;26(5-6):559-65.

The MAO-dependent inhibition of rotenone-insensitive NADH-cytochrome c-reductase and succinate dehydrogenase by biogenic amines, incubated with the mitochondrial fraction, was altered in the offspring of alcoholized animals as compared with control rats.
87(1,1,2,2) Details
15704879 Bufetov EN, Polygalova OO, Ponomareva AA: [Ultrastructural characteristics of mitochondria during cell adaptation to rotenone]. Tsitologiia. 2004;46(11):985-92.

Further on the normal ultrastructure of mitochondria was observed, which may result from activation of succinate dehydrogenase and rotenone resistant NAD (P) H-dehydrogenase.
81(1,1,1,1) Details
1664494 Benzi G, Curti D, Pastoris O, Marzatico F, Villa RF, Dagani F: Sequential damage in mitochondrial complexes by peroxidative stress. Neurochem Res. 1991 Dec;16(12):1295-302.

The cerebral peroxidative stress induces: (a) initially, a decrease in brain GSH concentration concomitant with a decrease in the mitochondrial activity of cytochrome oxidase of aa3-type (complex IV), without changes in ubiquinone and cytochrome b populations; (b) subsequently, an alteration in the transfer molecule cytochrome c and, finally, in rotenone-sensitive NADH-cytochrome c reductase (complex I) and succinate dehydrogenase (complex II).
37(0,1,2,2) Details
947364 Harmon HJ, Crane FL: Inhibition of mitochondrial electron transport by hydrophilic metal chelators. Biochim Biophys Acta. 1976 Jul 9;440(1):45-58.

The lack of succinate-indophenol reductase inhibition by bathophenanthroline sulfonate in the presence of rotenone or thenoyltrifluoroacetone indicates that the rotenone-sensitive site may be located on the matrix face and demonstrates that electrons flow between the NADH and succinate dehydrogenases via a hydrophilic chelator and rotenone-thenoyltrifluoroacetone-sensitive site on the matrix face of the membrane.
33(0,1,1,3) Details
7632092 Campos Y, Arenas J, Cabello A, Gomez-Reino JJ: Respiratory chain enzyme defects in patients with idiopathic inflammatory myopathy. Ann Rheum Dis. 1995 Jun;54(6):491-3.

Activity of rotenone sensitive NADH cytochrome c reductase (complex I and III) succinate dehydrogenase (complex II), succinate cytochrome c reductase (complex II and III), cytochrome c oxidase (complex IV), and citrate synthase (a mitochondrial matrix enzyme), was measured spectrophotometrically in muscle homogenates.
32(0,1,1,2) Details
2174585 Medvedev AE: [Regulation by biogenic amines of energy functions of mitochondria] . Vopr Med Khim. 1990 Sep-Oct;36(5):18-21.

Biogenic amines (phenylethylamine, tyramine, dopamine, tryptamine, serotonin and spermine) decreased activities of the rotenone-insensitive NADH-cytochrome c reductase, the succinate cytochrome c reductase and the succinate dehydrogenase in incubation mixtures containing mitochondrial membranes and the monoamine oxidase inhibitors chlorgyline and deprenyl.
32(0,1,1,2) Details
19495970 Villa RF, Gorini A, Hoyer S: Effect of Ageing and Ischemia on Enzymatic Activities Linked to Krebs' Cycle, Electron Transfer Chain, Glutamate and Aminoacids Metabolism of Free and Intrasynaptic Mitochondria of Cerebral Cortex. Neurochem Res. 2009 Jun 4.

The maximum rate (V (max)) of the following enzyme activities: citrate synthase, malate dehydrogenase, succinate dehydrogenase for Krebs' cycle; NADH-cytochrome c reductase as total (integrated activity of Complex I-III), rotenone sensitive (Complex I) and cytochrome oxidase (Complex IV) for electron transfer chain; glutamate dehydrogenase, glutamate-oxaloacetate- and glutamate-pyruvate transaminases for glutamate metabolism were assayed in non-synaptic, perikaryal mitochondria and in two populations of intra-synaptic mitochondria, i.e., the light and heavy mitochondrial fraction.
31(0,1,1,1) Details
15143528 Tkachenko HM, Moibenko OO, Kurhaliuk NM: [Effect of ATP-sensitive potassium channel modulators and intermittent hypoxia on mitochondrial respiration during stress]. Ukr Biokhim Zh. 2003 Nov-Dec;75(6):115-22.

We used next substrates of oxidation--0.35 mM succinate, 1 mM alpha-ketoglutarate, 3 mM glutamate, 3 mM pyruvate, 2.5 mM malate and inhibitor of the mitochondrial fermentative complex I (10 microM rotenone), succinate dehydrogenase inhibitor (2 mM malonate) and inhibitor of transamination (1 mM aminooxiacetate).
31(0,1,1,1) Details
1759390 Medvedev AE, Gorkin VZ: [The role of monoamine oxidase in the regulation of mitochondrial energy functions]. Vopr Med Khim. 1991 Sep-Oct;37(5):2-6.

Incubation of aldehyde dehydrogenase-free mitochondrial preparations with biogenic amines serotonin, tyramine, 2-phenylethylamine and 5-methoxytryptamine resulted in inhibition of enzymes activity of both outer (rotenone-insensitive NADH-cytochrome c reductase) and inner (succinate dehydrogenase, succinate cytochrome c reductase) mitochondrial membranes.
31(0,1,1,1) Details
9065733 Ferreira FM, Madeira VM, Moreno AJ: Interactions of 2,2-bis (p-chlorophenyl)-1,1-dichloroethylene with mitochondrial oxidative phosphorylation. Biochim Biophys Acta. 1976 Aug 23;441(2):231-8.

In addition, data from carbonyl cyanide m-chlorophenylhydrazone-uncoupled rotenone-inhibited preparations or submitochondrial particles indicated that F0F1 ATPase activity is not affected by DDE.
In fact, DDE interacted with succinate dehydrogenase (complex II), decreasing respiration and membrane potential.
1(0,0,0,1) Details
16686429 Lopez-Barneo J, Ortega-Saenz P, Piruat JI, Garcia-Fernandez M: Oxygen-sensing by ion channels and mitochondrial function in carotid body glomus cells. Novartis Found Symp. 2006;272:54-64; discussion 64-72

However, rotenone, a complex I blocker, selectively occludes the responsiveness to hypoxia of glomus cells in a dose-dependent manner.
We have also generated a knock-out mouse lacking SDHD, the small membrane-anchoring protein of the succinate dehydrogenase (complex II) of the mitochondrial electron transport chain.
1(0,0,0,1) Details
14681995 Tkachenko HM, Kurhaliuk NM, Vovkanych LS: [Role of ATP-sensitive potassium channel activators in liver mitochondrial function in rats with different resistance to hypoxia]. Ukr Biokhim Zh. 2003 Sep-Oct;75(5):69-76.

Additional analyses contain the next inhibitors: mitochondrial fermentative complex I-10 mkM rotenone, succinate dehydrogenase 2 mM malonic acid.
31(0,1,1,1) Details
12632423 Maneiro E, Martin MA, de Andres MC, Lopez-Armada MJ, Fernandez-Sueiro JL, del Hoyo P, Galdo F, Arenas J, Blanco FJ: Mitochondrial respiratory activity is altered in osteoarthritic human articular chondrocytes. Arthritis Rheum. 2003 Mar;48(3):700-8.

The activities of mitochondrial respiratory chain complexes (complex I: rotenone-sensitive NADH-coenzyme Q (1) reductase; complex II: succinate dehydrogenase; complex III: antimycin-sensitive ubiquinol cytochrome c reductase; and complex IV: cytochrome c oxidase) and CS were measured in human articular chondrocytes isolated from OA and normal cartilage.
31(0,1,1,1) Details
10844979 Obungu VH, Kiaira JK, Olembo NK, Njogu MR: Pathways of glucose catabolism in procyclic Trypanosoma congolense. Indian J Biochem Biophys. 1999 Oct;36(5):305-11.

Studies of respiration on glucose in procyclic Trypanosoma congolense in the presence of rotenone, antimycin, cyanide, salicylhydroxamic acid and malonate have indicated the presence of NADH dehydrogenase, cytochrome b-c1, cytochrome aa3, trypanosome alternate oxidase and NADH fumarate reductase/succinate dehydrogenase pathway that contributes electrons to coenzyme Q of the respiratory chain.
7(0,0,1,2) Details
22598 Della Corte L, Callingham BA: The influence of adrenalectomy on monoamine oxidase and NADH cytochrome c reductase in the rat heart. Biochim Biophys Acta. 1975 Dec 11;408(3):284-96.

The effect of adrenalectomy on the activities of monoamine oxidase (MAO), NADH cytochrome c reductase (NCR), succinate dehydrogenase, malate dehydrogenase, fumarase, NAD+ nucleosidase and acid phosphatase in homogenates of rat hearts was examined.
However, both the total and the rotenone-insensitive NCR activities increased, with that of the rotenone-insensitive being about half of the total, which indicated that the effect of adrenalectomy was exerted on components of this enzyme localized on both the inner and outer membranes of the mitochondrion.
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1171697 Wang CC: Studies of the mitochondria from Eimeria tenella and inhibition of the electron transport by quinolone coccidiostats. Biochim Biophys Acta. 1975 Aug 11;396(2):210-9.

They inhibited submitochondrial succinate dehydrogenase and NADH dehydrogenase of E. tenella, and remained equally active against the mitochondrial function of E. tenella amquinolate-resistant mutant.
The mitochondrial respiration was inhibited by cyanide, azide, carbon monoxide, antimycin A, and 2-heptyl-4-hydroxyquinoline-N-oxide, but was relatively resistant to rotenone and amytal.
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17011837 Bacsi A, Woodberry M, Widger W, Papaconstantinou J, Mitra S, Peterson JW, Boldogh I: Localization of superoxide anion production to mitochondrial electron transport chain in 3-NPA-treated cells. Mitochondrion. 2006 Oct;6(5):235-44. Epub 2006 Aug 3.

3-Nitropropionic acid (3-NPA), an inhibitor of succinate dehydrogenase (SDH) at complex II of the mitochondrial electron transport chain induces cellular energy deficit and oxidative stress-related neurotoxicity.
In the present study, we identified the site of reactive oxygen species production in mitochondria. 3-NPA increased O2- generation in mitochondria respiring on the complex I substrates pyruvate+malate, an effect fully inhibited by rotenone.
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9264320 Dong Y, Berners-Price SJ, Thorburn DR, Antalis T, Dickinson J, Hurst T, Qiu L, Khoo SK, Parsons PG: Serine protease inhibition and mitochondrial dysfunction associated with cisplatin resistance in human tumor cell lines: targets for therapy. Biochem Pharmacol. 1997 Jun 1;53(11):1673-82.

Unlike the HeLa clones, CI-80-13S cells were additionally sensitive to chloramphenicol, 1-methyl-4-phenylpyridinium ion (MPP+), rotenone, thenoyltrifluoroacetone (TTFA), and antimycin A, and showed poor reduction of 1-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide (MTT), suggesting a deficiency in NADH dehydrogenase and/or succinate dehydrogenase activities.
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3426243 Hohl C, Oestreich R, Rosen P, Wiesner R, Grieshaber M: Evidence for succinate production by reduction of fumarate during hypoxia in isolated adult rat heart cells. Arch Biochem Biophys. 1987 Dec;259(2):527-35.

Moreover, anaerobic succinate formation was rotenone sensitive.
We conclude that malate reduction to succinate occurs via the reverse action of succinate dehydrogenase in a coupled reaction where NADH is oxidized (and FAD reduced) and ADP is phosphorylated.
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8158142 Veuthey AL, Tsacopoulos M, Millan de Ruiz L, Perrottet P: Cellular and subcellular localization of hexokinase, glutamate dehydrogenase, and alanine aminotransferase in the honeybee drone retina. J Neurochem. 1994 May;62(5):1939-46.

The distribution of enzymatic markers of mitochondria (succinate dehydrogenase, rotenone-insensitive cytochrome c reductase, and adenylate kinase) indicated that the outer mitochondrial membrane was partly damaged, but their distributions were different from that of hexokinase.
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494532 Kamysheva AS, Pigareva ZD: [Mitochondrial energy processes of the visual system in the rabbit brain normally and under conditions of light deprivation]. Vopr Med Khim. 1979 Sep-Oct;25(5):515-20.


The mitochondria of experimental rabbits were characterized by distinct alteration in oxidative phosphorylation of glutamic acid, by an increased rate of electron transport at the step between cytochrome c-cytochrome oxidase-succinate dehydrogenase of the respiratory chain as well as by the peculiar effect of rothenone and DNP on the chain.
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10841308 de Halac IN, Bacman SR, de Kremer RD: Histoenzymology of oxidases and dehydrogenases in peripheral blood lymphocytes and monocytes for the study of mitochondrial oxidative phosphorylation. Histochem J. 2000 Mar;32(3):133-7.

The specificity of each histoenzymological reaction was tested using a specific respiratory chain inhibitor: rotenone for NADH diaphorase, thenoyltrifluoroacetone for succinate dehydrogenase, potassium cyanide for cytochrome c oxidase and oligomycin for ATPase.
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1567448 Unnikrishnan LS, Raj RK: Fumarate reductase system of filarial parasite Setaria digitata. Biochem Biophys Res Commun. 1992 Apr 15;184(1):448-53.

This activity is sensitive to rotenone, antimycin A and o-Hydroxy diphenyl.
The fumarate reductase system consisting of NADH-coenzyme Q reductase, cytochrome b like component (s) and succinate dehydrogenase/fumarate reductase is thus very important and hence specific inhibitors of the system may prove useful in the effective control of filariasis.
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11167513 Piasecka M, Wenda-Rozewicka L, Ogonski T: Computerized analysis of cytochemical reactions for dehydrogenases and oxygraphic studies as methods to evaluate the function of the mitochondrial sheath in rat spermatozoa. Andrologia. 2001 Jan;33(1):1-12.


Cytochemical reactions for mitochondrial NADH-dependent dehydrogenases (diaphorase/NADH which is related to flavoprotein), NAD-dependent dehydrogenases (isocitrate, malate) and succinate dehydrogenase were carried out in rat spermatozoa.
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