| Name | NADH:ubiquinone oxidoreductase (protein family or complex) |
|---|---|
| Synonyms | NADH ubiquinone oxidoreductase; NADH ubiquinone oxidoreductases; NADH:ubiquinone oxidoreductase; NADH:ubiquinone oxidoreductases |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 15450959 | Cardol P, Vanrobaeys F, Devreese B, Van Beeumen J, Matagne RF, Remacle C: Higher plant-like subunit composition of mitochondrial complex I from Chlamydomonas reinhardtii: 31 conserved components among eukaryotes. Biochim Biophys Acta. 2004 Oct 4;1658(3):212-24. The rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) is the most intricate membrane-bound enzyme of the mitochondrial respiratory chain. |
6(0,0,1,1) | Details |
| 19097788 | Dong CK, Patel V, Yang JC, Dvorin JD, Duraisingh MT, Clardy J, Wirth DF: Type II NADH dehydrogenase of the respiratory chain of Plasmodium falciparum and its inhibitors. Bioorg Med Chem Lett. 2009 Feb 1;19(3):972-5. Epub 2008 Nov 24. Plasmodium falciparum NDH2 (pfNDH2) is a non- pumping, rotenone-insensitive alternative enzyme to the multi-subunit NADH:ubiquinone oxidoreductases (Complex I) of many other eukaryotes. |
6(0,0,1,1) | Details |
| 1900238 | Marres CA, de Vries S, Grivell LA: Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur J Biochem. 1991 Feb 14;195(3):857-62. We have recently described the isolation of a mitochondrial rotenone-insensitive NADH:ubiquinone oxidoreductase from Saccharomyces cerevisiae [de Vries, S. & Grivell, L. |
6(0,0,1,1) | Details |
| 11671409 | Fang N, Casida JE: Novel Bioactive Cube Insecticide Constituents: Isolation and Preparation of 13-homo-13-Oxa-6a,12a-dehydrorotenoids. J Org Chem. 1997 Jan 24;62(2):350-353. Compound 5 from cube resin was identical with a product previously reported as being formed by reaction of rotenone (1) with acetyl and DMF and misassigned as "6a,12a-epoxyrotenone" (7). Rotenoid 5 acts as a respiratory inhibitor with 50% inhibition of NADH:ubiquinone oxidoreductase activity at 0.11 &mgr;M, of goldfish survival at 1 ppm, and of the viability of three cell lines at 4-8 &mgr;M. |
1(0,0,0,1) | Details |
| 15540952 | Caboni P, Sherer TB, Zhang N, Taylor G, Na HM, Greenamyre JT, Casida JE: Rotenone, deguelin, their metabolites, and the rat model of Parkinson's disease. Chem Res Toxicol. 2004 Nov;17(11):1540-8. They are also potent complex I (NADH:ubiquinone oxidoreductase) inhibitors. |
1(0,0,0,1) | Details |
| 14670598 | Grivennikova VG, Roth R, Zakharova NV, Hagerhall C, Vinogradov AD: The mitochondrial and prokaryotic -translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the -junction sites. Biochim Biophys Acta. 2003 Dec 8;1607(2-3):79-90. The catalytic properties of the rotenone-sensitive NADH:ubiquinone reductase (Complex I) in bovine heart submitochondrial particles and in inside-out vesicles derived from Paracoccus denitrificans and Rhodobacter capsulatus were compared. |
1(0,0,0,1) | Details |
| 18445136 | Kilbride SM, Telford JE, Tipton KF, Davey GP: Partial inhibition of complex I activity increases Ca-independent release rates from depolarized synaptosomes. J Neurochem. 2008 Jul;106(2):826-34. Epub 2008 Apr 28. Mitochondria have been implicated in the pathogenesis of several neurodegenerative disorders and, in particular, complex I (NADH:ubiquinone oxidoreductase, EC 1.6.5.3) activity has been shown to be partially reduced in postmortem studies of the substantia nigra of Parkinson's disease patients. Following a 40% inhibition of complex I activity with rotenone, it was found that Ca (2+)-independent release of increased from synaptosomes depolarized with 4-aminopyridine. |
1(0,0,0,1) | Details |
| 1959619 | Majander A, Huoponen K, Savontaus ML, Nikoskelainen E, Wikstrom M: Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 1991 Nov 4;292(1-2):289-92. We report the electron transfer properties of the NADH:ubiquinone oxidoreductase complex of the respiratory chain (Complex I) in mitochondria of cells derived from LHON patients with two different mutations in mitochondrial DNA (mtDNA). The ND1/3460 mutation exhibits 80% reduction in rotenone-sensitive and -dependent electron transfer activity, whereas the proximal NADH dehydrogenase activity of the Complex is unaffected. |
1(0,0,0,1) | Details |
| 2539917 | Rossi SC, Wetterhahn KE: (V) is produced upon reduction of chromate by mitochondrial electron transport chain complexes. Carcinogenesis. 1989 May;10(5):913-20. Rotenone, antimycin and all produced approximately 40% inhibition of the -dependent chromate-reductase activity. Thus, complex I (NADH:ubiquinone oxidoreductase) appears to be responsible for the inhibitor-insensitive, and complex IV (ferrocytochrome c:oxygen oxidoreductase) for the inhibitor-sensitive -dependent (VI) reduction and (V) formation. |
1(0,0,0,1) | Details |
| 8307034 | Friedrich T, van Heek P, Leif H, Ohnishi T, Forche E, Kunze B, Jansen R, Trowitzsch-Kienast W, Hofle G, Reichenbach H, et al.: Two binding sites of inhibitors in oxidoreductase (complex I). Eur J Biochem. 1994 Jan 15;219(1-2):691-8. The effect of ten naturally occurring and two synthetic inhibitors of NADH:ubiquinone oxidoreductase (complex I) of bovine heart, Neurospora crassa and Escherichia coli and glucose:ubiquinone oxidoreductase (glucose dehydrogenase) of Gluconobacter oxidans was investigated. Class II inhibitors including the naturally occurring rotenone, phenoxan, aureothin and the synthetic benzimidazole inhibit complex I from all species in an non-competitive manner, but have no effect on the glucose dehydrogenase. |
1(0,0,0,1) | Details |
| 18037377 | Gostimskaya IS, Grivennikova VG, Cecchini G, Vinogradov AD: Reversible dissociation of from the mammalian membrane-bound oxidoreductase (complex I). FEBS Lett. 2007 Dec 22;581(30):5803-6. Epub 2007 Nov 26. Conditions for the reversible dissociation of from the membrane-bound mitochondrial NADH:ubiquinone oxidoreductase (complex I) are described. The catalytic activities of the enzyme, i.e. rotenone-insensitive NADH:hexaammineruthenium III reductase and rotenone-sensitive NADH:quinone reductase decline when bovine heart submitochondrial particles are incubated with in the presence of rotenone or at alkaline pH. |
1(0,0,0,1) | Details |
| 15248896 | DeHaan C, Habibi-Nazhad B, Yan E, Salloum N, Parliament M, Allalunis-Turner J: Mutation in mitochondrial complex I ND6 subunit is associated with defective response to hypoxia in human glioma cells. Mol Cancer. 2004 Jul 12;3:19. RESULTS: The mitochondrial genome was sequenced and 23 mtDNA alterations were identified, one of which was an unreported mutation (T-C transition in base pair 14634) in the hypoxia-sensitive cell line, M010b, that resulted in a single amino acid change in the gene encoding the ND6 subunit of NADH:ubiquinone oxidoreductase (Complex I). The T14634C mutation did not abrogate ND6 protein expression, however, M010b cells were more resistant to rotenone, an agent used to screen for Complex I mutations, and adriamycin, an agent activated by redox cycling. |
1(0,0,0,1) | Details |
| 9520374 | Fang N, Casida JE: Anticancer action of cube insecticide: correlation for rotenoid constituents between inhibition of NADH:ubiquinone oxidoreductase and induced ornithine decarboxylase activities. Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3380-4. The toxic action of rotenone is attributed to inhibition of NADH:ubiquinone oxidoreductase activity and the purported cancer chemopreventive effect of deguelin analogs has been associated with inhibition of phorbol ester-induced ornithine decarboxylase (ODC) activity. |
165(2,2,2,5) | Details |
| 8856105 | Ueno H, Miyoshi H, Inoue M, Niidome Y, Iwamura H: Structural factors of rotenone required for inhibition of various NADH-ubiquinone oxidoreductases. Biochim Biophys Acta. 1996 Sep 30;1276(3):195-202. |
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| 12411515 | Hanley PJ, Ray J, Brandt U, Daut J: Halothane, isoflurane and sevoflurane inhibit NADH:ubiquinone oxidoreductase (complex I) of cardiac mitochondria. J Physiol. 2002 Nov 1;544(Pt 3):687-93. 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. |
5(0,0,0,5) | Details |
| 8063722 | Majander A, Finel M, Wikstrom M: Diphenyleneiodonium inhibits reduction of iron- clusters in the mitochondrial NADH-ubiquinone oxidoreductase (Complex I). J Biol Chem. 1994 Aug 19;269(33):21037-42. Similar results were found with Complex I and two rotenone-insensitive preparations, subcomplex I lambda and the flavoprotein fraction. |
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| 15175007 | Lambert AJ, Brand MD: production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem J. 2004 Sep 1;382(Pt 2):511-7. By far, the largest rate of production was from mitochondria respiring on this rate was almost abolished by rotenone or piericidin, indicating that production from complex I is large under conditions of reverse electron transport. |
1(0,0,0,1) | Details |
| 10552508 | Fang N, Casida JE: Cube resin insecticide: identification and biological activity of 29 rotenoid constituents. J Agric Food Chem. 1999 May;47(5):2130-6. The four major active ingredients are rotenone, deguelin, rotenolone, and tephrosin, totaling 77 wt %. Assays of the 29 rotenoids as inhibitors of NADH:ubiquinone oxidoreductase activity (primary target for toxicity) and phorbol ester-induced ornithine decarboxylase activity (indicator of cancer chemopreventive action) and for cytotoxicity establish similar structure-activity relationships in each system and the importance of the overall molecular conformation and the E-ring substituents. |
1(0,0,0,1) | Details |
| 11358527 | Fang J, Wang Y, Beattie DS: Isolation and characterization of complex I, rotenone-sensitive oxidoreductase, from the procyclic forms of Trypanosoma brucei. Eur J Biochem. 2001 May;268(10):3075-82. Both proline:cytochrome c reductase and NADH:ubiquinone oxidoreductase of procyclic T. brucei were inhibited by the specific inhibitors of complex I rotenone, piericidin A, and |
93(1,1,3,3) | Details |
| 15215104 | Mills SD, Yang W, MacCormack K: Molecular characterization of benzimidazole resistance in Helicobacter pylori. Antimicrob Agents Chemother. 2004 Jul;48(7):2524-30. MIC testing of the wild-type H. pylori strain and four classes of nuo mutants revealed that all NuoD mutant classes were hypersensitive to rotenone, a known inhibitor of complex I (NADH:ubiquinone oxidoreductase) suggested to bind to NuoD. |
82(1,1,1,2) | Details |
| 14727190 | Gonzalez-Halphen D, Maslov DA: NADH-ubiquinone oxidoreductase activity in the kinetoplasts of the plant trypanosomatid Phytomonas serpens. Parasitol Res. 2004 Mar;92(4):341-6. Epub 2004 Jan 16. Rotenone at 2-10 microM inhibited the activity 50-75%, indicating that it belongs to respiratory complex I. |
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| 8443212 | Sled VD, Vinogradov AD: Kinetics of the mitochondrial NADH-ubiquinone oxidoreductase interaction with hexammineruthenium (III). Biochim Biophys Acta. 1993 Mar 1;1141(2-3):262-8. Both hexammineruthenium (III) and ferricyanide reduction was rotenone-insensitive and showed no stimulation by the uncouplers in tightly coupled submitochondrial particles. |
3(0,0,0,3) | Details |
| 8804429 | Finel M: Genetic inactivation of the H (+)-translocating NADH:ubiquinone oxidoreductase of Paracoccus denitrificans is facilitated by insertion of the ndh gene from Escherichia coli. FEBS Lett. 1996 Sep 9;393(1):81-5. Subsequent homologous recombination gave rise to a mutant the membranes of which catalyzed rotenone-insensitive oxidation, but which did not oxidize deamino- |
3(0,0,0,3) | Details |
| 9230920 | Zharova TV, Vinogradov AD: A competitive inhibition of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) by ADP- Biochim Biophys Acta. 1997 Jul 4;1320(3):256-64. Ki for inhibition of the rotenone-sensitive oxidase in SMP by ADPR does not depend on delta mu H+. |
1(0,0,0,1) | Details |
| 10462447 | Tormo JR, Gonzalez MC, Cortes D, Estornell E: Kinetic characterization of mitochondrial complex I inhibitors using annonaceous acetogenins. Arch Biochem Biophys. 1999 Sep 1;369(1):119-26. The NADH:ubiquinone oxidoreductase (complex I) of the mitochondrial respiratory chain is by far the largest and most complicated of the -translocating enzymes involved in the oxidative phosphorylation. |
1(0,0,0,1) | Details |
| 19073440 | King TD, Clodfelder-Miller B, Barksdale KA, Bijur GN: Unregulated mitochondrial GSK3beta activity results in oxidoreductase deficiency. Neurotox Res. 2008 Dec;14(4):367-82. Here we selectively expressed constitutively active GSK3beta within the mitochondria and found that this enhanced the apoptosis signaling activated by the PD-mimetic NADH:ubiquinone oxidoreductase (complex I) inhibitors 1-methyl-4-phenylpyridinium ion (MPP+) and rotenone. |
81(1,1,1,1) | Details |
| 11245783 | Prieur I, Lunardi J, Dupuis A: Evidence for a binding site close to the interface between NUOD and NUOB subunits of Complex I. Biochim Biophys Acta. 2001 Apr 2;1504(2-3):173-8. Piericidin, rotenone and pyridaben are specific inhibitors of the NADH-ubiquinone oxidoreductase (Complex I) that bind to its binding site (s). |
81(1,1,1,1) | Details |
| 16777535 | van der Merwe JA, Dubery IA: Benzothiadiazole inhibits mitochondrial NADH:ubiquinone oxidoreductase in tobacco. J Plant Physiol. 2006 Jul;163(8):877-82. Epub 2005 Nov 9. Using a dichlorodihydrofluorescein assay, it was found that benzothiadiazole, and the complex I inhibitor rotenone, increased reactive species production within cells in a concentration-dependent manner. |
3(0,0,0,3) | Details |
| 17530440 | Liu Y, Qiao DR, Zheng HB, Dai XL, Bai LH, Zeng J, Cao Y: Cloning and sequence analysis of the gene encoding 19-kD subunit of Complex I from Dunaliella salina. Mol Biol Rep. 2008 Sep;35(3):397-403. Epub 2007 May 26. NADH:ubiquinone oxidoreductase (complex I ) of the mitochondrial respiratory chain catalyzes the transfer of electrons from to coupled to translocation across the membrane. The 19-kD subunit mRNA expression was observed in oxygen deficiency, salt treatment, and rotenone treatment with lower levels. |
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| 18486594 | Fendel U, Tocilescu MA, Kerscher S, Brandt U: Exploring the inhibitor binding pocket of respiratory complex I. . Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):660-5. Epub 2008 Apr 30. Numerous hydrophobic and amphipathic compounds including several detergents are known to inhibit the ubiquinone reductase reaction of respiratory chain complex I pumping NADH:ubiquinone oxidoreductase). Many mutations around the domain of the 49-kDa subunit that is homologous to the [NiFe] centre binding region of hydrogenase conferred resistance to DQA (class I/type A) and rotenone (class II/type B) indicating a wider overlap of the binding sites for these two types of inhibitors. |
1(0,0,0,1) | Details |
| 8206244 | Jewess PJ: Insecticides and acaricides which act at the rotenone-binding site of mitochondrial NADH:ubiquinone oxidoreductase; competitive displacement studies using a 3H-labelled rotenone analogue. Biochem Soc Trans. 1994 Feb;22(1):247-51. |
81(1,1,1,1) | Details |
| 9684860 | Darrouzet E, Issartel JP, Lunardi J, Dupuis A: The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two -related inhibitors. FEBS Lett. 1998 Jul 10;431(1):34-8. |
32(0,1,1,2) | Details |
| 12171069 | Magnitsky S, Toulokhonova L, Yano T, Sled VD, Hagerhall C, Grivennikova VG, Burbaev DS, Vinogradov AD, Ohnishi T: EPR characterization of ubisemiquinones and iron- cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ. J Bioenerg Biomembr. 2002 Jun;34(3):193-208. In the current study, special attention was placed on the SQNf, because of its high sensitivities to DeltamicroH+ and to specific complex I inhibitors (rotenone and piericidin A) in a unique manner. |
2(0,0,0,2) | Details |
| 11418099 | Schuler F, Casida JE: Functional coupling of PSST and ND1 subunits in NADH:ubiquinone oxidoreductase established by photoaffinity labeling. Biochim Biophys Acta. 2001 Jul 2;1506(1):79-87. |
2(0,0,0,2) | Details |
| 17289351 | Verkaart S, Koopman WJ, van Emst-de Vries SE, Nijtmans LG, van den Heuvel LW, Smeitink JA, Willems PH: production is inversely related to complex I activity in inherited complex I deficiency. Biochim Biophys Acta. 2007 Mar;1772(3):373-81. Epub 2007 Jan 4. Deficiency of NADH:ubiquinone oxidoreductase or complex I (CI) is the most common cause of disorders of the oxidative phosphorylation system in humans. In agreement with this finding, rotenone, a potent inhibitor of CI activity, dose-dependently increased production in healthy control cells. |
1(0,0,0,1) | Details |
| 16798828 | Andrukhiv A, Costa AD, West IC, Garlid KD: Opening mitoKATP increases generation from complex I of the electron transport chain. Am J Physiol Heart Circ Physiol. 2006 Nov;291(5):H2067-74. Epub 2006 Jun 23. This indicates that the originates in complex I (NADH:ubiquinone oxidoreductase) of the electron transport chain. Myxothiazol stimulated mitoK (ATP)-dependent ROS production, whereas rotenone had no effect. |
1(0,0,0,1) | Details |
| 10747996 | Scacco S, Vergari R, Scarpulla RC, Technikova-Dobrova Z, Sardanelli A, Lambo R, Lorusso V, Papa S: cAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures. J Biol Chem. 2000 Jun 9;275(23):17578-82. Phosphorylation of the 18-kDa subunit, in response to cholera toxin treatment of fibroblasts, was accompanied by a 2-3-fold enhancement of the rotenone-sensitive endogenous respiration of fibroblasts, of the rotenone-sensitive oxidase, and of the NADH:ubiquinone oxidoreductase activity of complex I. |
32(0,1,1,2) | Details |
| 16895522 | Sherwood S, Hirst J: Investigation of the mechanism of translocation by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria: does the enzyme operate by a Q-cycle mechanism?. Biochem J. 2006 Dec 15;400(3):541-50. Unexpectedly, in the presence of complex I inhibited by either rotenone or piericidin A was found to catalyse the exchange of redox states between different and species, providing a possible route for future investigations into the mechanism of energy transduction. |
2(0,0,0,2) | Details |
| 9282833 | Fang N, Rowlands JC, Casida JE: Anomalous structure-activity relationships of 13-homo-13-oxarotenoids and 13-homo-13-oxadehyrorotenoids. Chem Res Toxicol. 1997 Aug;10(8):853-8. Cube resin, used as an insecticide/miticide and piscicide, contains in decreasing amounts rotenone (1), deguelin (2), the 6a,12a-dehydro derivatives of rotenone (3) and deguelin (4), and the newly-discovered 13-homo-13-oxa-6a,12a-dehydro analogs [referred to as oxadehydrorotenone (5) and -deguelin (6)]. These six rotenoids were compared for potency as inhibitors of NADH:ubiquinone oxidoreductase activity and for organismal toxicity to mosquito larvae, goldfish, and mice and cytotoxicity in three mammalian cell lines (Hepa 1C1C7, MCF 7, and NB 41A3). |
2(0,0,0,2) | Details |
| 15849190 | Pineau B, Mathieu C, Gerard-Hirne C, De Paepe R, Chetrit P: Targeting the NAD7 subunit to mitochondria restores a functional complex I and a wild type phenotype in the Nicotiana sylvestris CMS II mutant lacking nad7. J Biol Chem. 2005 Jul 15;280(28):25994-6001. Epub 2005 Apr 22. The mitochondrial DNA of the Nicotiana sylvestris CMSII mutant carries a 72-kb deletion comprising the single copy nad7 gene that encodes the NAD7 subunit of the respiratory complex I (NADH-ubiquinone oxidoreductase). CMSII plants lack rotenone-sensitive complex I activity and are impaired in physiological and phenotypical traits. |
1(0,0,0,1) | Details |
| 9092484 | Miyako K, Kai Y, Irie T, Takeshige K, Kang D: The content of intracellular mitochondrial DNA is decreased by 1-methyl-4-phenylpyridinium ion (MPP+). J Biol Chem. 1997 Apr 11;272(15):9605-8. 1-Methyl-4-phenylpyridinium ion (MPP+), an oxidative metabolite of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is considered to be directly responsible for MPTP-induced Parkinson's disease-like symptoms by inhibiting NADH-ubiquinone oxidoreductase (complex I) in the mitochondrial respiratory chain. On the contrary, 0.1 microM rotenone, which inhibits complex I to the same extent as 25 microM MPP+ in the cells, increases the content of mitochondrial DNA about 2-fold. |
1(0,0,0,1) | Details |
| 6517863 | Earley FG, Ragan CI: Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone. Biochem J. 1984 Dec 1;224(2):525-34. The analogue inhibits NADH-ubiquinone oxidoreductase activity at concentrations comparable with those of rotenone. |
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| 8839048 | Latli B, Wood E, Casida JE: Insecticidal quinazoline derivatives with (trifluoromethyl) diazirinyl and azido substituents as NADH:ubiquinone oxidoreductase inhibitors and candidate photoaffinity probes. Chem Res Toxicol. 1996 Mar;9(2):445-50. Two candidate photoaffinity probes are designed from 4-substituted quinazolines known to be potent insecticides/acaricides and NADH:ubiquinone oxidoreductase inhibitors acting at or near the rotenone site. 4-(11-Azidoundecyl-2-amino) quinazoline, based on the undecylamino analog SAN 548A as a prototype, was synthesized in 18% overall yield from ethyl 10-undecenoate by oxidation of the terminal double bond, reductive amination, coupling to 4-chloroquinazoline, and functional group manipulation of the terminal ethyl ester to an a mesylate and finally nucleophilic displacement with azide ions. 4-(4-(3-(Trifluoromethyl)-3H-diazirin-3-yl) phenethoxy) quinaz oline [the (trifluoromethyl) diazirinyl analog of fenazaquin insecticide/acaricide] was prepared from 4-bromophenethyl in 31% overall yield by first introducing the trifluoromethylketone moiety followed by its conversion to the (trifluoromethyl)-diazirine and finally coupling to 4-chloroquinazoline as above. |
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| 12914921 | Grivennikova VG, Ushakova AV, Cecchini G, Vinogradov AD: Unidirectional effect of lauryl on the reversible NADH:ubiquinone oxidoreductase (Complex I). FEBS Lett. 2003 Aug 14;549(1-3):39-42. The inhibitor affects neither oxidase (coupled or uncoupled) nor NADH:ferricyanide reductase and oxidase activities at the concentrations that selectively prevent the -supported, rotenone-sensitive (+) or ferricyanide reduction. |
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| 10417649 | Krebs W, Steuber J, Gemperli AC, Dimroth P: Na+ translocation by the NADH:ubiquinone oxidoreductase (complex I) from Klebsiella pneumoniae. Mol Microbiol. 1999 Aug;33(3):590-8. The uptake of ions was severely inhibited by the complex I-specific inhibitor rotenone with deaminoNADH or as substrate. |
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| 7941733 | Buschges R, Bahrenberg G, Zimmermann M, Wolf K: oxidoreductase in obligate aerobic yeasts. Yeast. 1994 Apr;10(4):475-9. The strictly aerobic yeasts Candida pinus, Cryptococcus albidus, Rhodotorula minuta, Rhodotorula mucilaginosa and Trichosporon beigelii possess mitochondrial NADH dehydrogenases with significant features of the NADH:ubiquinone oxidoreductase (complex I). These species show in all growth phases and under standard cultivation conditions, NADH dehydrogenases of approximately 700 kDa, which are sensitive to rotenone, a specific inhibitor of this complex. |
1(0,0,0,1) | Details |
| 17760425 | Grivennikova VG, Kotlyar AB, Karliner JS, Cecchini G, Vinogradov AD: Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I. Biochemistry. 2007 Sep 25;46(38):10971-8. Epub 2007 Aug 31. A very potent and specific inhibitor of mitochondrial NADH:ubiquinone oxidoreductase (complex I), a derivative of -OH) has recently been discovered (Kotlyar, A. The effect of is completely reversed by rotenone, antimycin A, and uncoupler. |
1(0,0,0,1) | Details |
| 16893179 | Murai M, Ichimaru N, Abe M, Nishioka T, Miyoshi H: Mode of inhibitory action of Deltalac-acetogenins, a new class of inhibitors of bovine heart mitochondrial complex I. Biochemistry. 2006 Aug 15;45(32):9778-87. We have revealed that Deltalac-acetogenins, a new class of inhibitors of bovine heart mitochondrial complex I (NADH-ubiquinone oxidoreductase), act differently from ordinary inhibitors such as rotenone and piericidin A [Ichimaru et al. (2005) Biochemistry 44, 816-825]. |
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| 9305406 | Klohn PC, Neumann HG: Impairment of respiration and oxidative phosphorylation by redox cyclers 2-nitrosofluorene and Chem Biol Interact. 1997 Aug 29;106(1):15-28. NOF reacts with the NADH:ubiquinone oxidoreductase (complex I) and consumes in a rotenone-insensitive manner. |
31(0,1,1,1) | Details |
| 10876012 | Chowdhury SK, Drahota Z, Floryk D, Calda P, Houstek J: Activities of mitochondrial oxidative phosphorylation enzymes in cultured amniocytes. Clin Chim Acta. 2000 Aug;298(1-2):157-73. In this paper, we present a complex protocol for evaluation of the function of mitochondrial OXPHOS enzymes in cultured amniocytes using three independent and complementary methods: (a) spectrophotometry as a tool for determination of the capacities of mitochondrial respiratory-chain enzymes (NADH ubiquinone oxidoreductase, - and glycerophosphate cytochrome c reductase, cytochrome c oxidase and citrate synthase); (b) polarography as a tool for the evaluation of mitochondrial OXPHOS enzyme functions in situ using digitonin-permeabilised amniocytes (rotenone-sensitive oxidation of pyruvate+malate, antimycin A-sensitive oxidation of KCN-sensitive oxidation of cytochrome c, -activated substrate oxidation) and (c) cytofluorometric determination of tetramethyl rhodamine methyl ester (TMRM) fluorescence in digitonin-permeabilised amniocytes as a sensitive way to determine the mitochondrial membrane potential under steady-state conditions (state 4 with |
31(0,1,1,1) | Details |
| 8573592 | Satoh T, Miyoshi H, Sakamoto K, Iwamura H: Comparison of the inhibitory action of synthetic analogues with various NADH-ubiquinone oxidoreductases. Biochim Biophys Acta. 1996 Jan 11;1273(1):21-30. Some synthetic capsaicins were fairly potent inhibitors of each of the three NDH-1 compared with the potent rotenone and piericidin A. |
2(0,0,0,2) | Details |
| 8313963 | Finel M, Majander A: Studies on the -translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10-phenanthroline. FEBS Lett. 1994 Feb 14;339(1-2):142-6. EPR spectroscopy of submitochondrial particles indicates that OP, similarly to rotenone, inhibits electron transfer between the Fe-S clusters of complex I and the pool. |
2(0,0,0,2) | Details |
| 17477844 | Zoccarato F, Cavallini L, Bortolami S, Alexandre A: modulation of H2O2 release at NADH:ubiquinone oxidoreductase (Complex I) in brain mitochondria. Biochem J. 2007 Aug 15;406(1):125-9. The much faster -dependent H2O2 production is ascribed to Complex I, being rotenone-sensitive. |
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| 10869199 | Guadano A, Gutierrez C, de La Pena E, Cortes D, Gonzalez-Coloma A: Insecticidal and mutagenic evaluation of two annonaceous acetogenins. J Nat Prod. 2000 Jun;63(6):773-6. Annonaceous acetogenins represent a new class of bioactive compounds whose primary mode of action is the inhibition of NADH-ubiquinone oxidoreductase. We compared these results with those obtained with rotenone, a well-known respiratory inhibitor that was highly toxic to L. decemlineata and M. persicae and showed no mutagenicity/toxicity in the S. typhimurium strains tested up to a concentration of 1000 microg per plate. |
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| 11080300 | Sabar M, De Paepe R, de Kouchkovsky Y: Complex I impairment, respiratory compensations, and photosynthetic decrease in nuclear and mitochondrial male sterile mutants of Nicotiana sylvestris. Plant Physiol. 2000 Nov;124(3):1239-50. We have previously shown that in Nicotiana sylvestris cytoplasmic male-sterile (CMS) mutants where the mtDNA lacks the nad7 gene coding for a subunit of respiratory Complex I (NADH:ubiquinone oxidoreductase, EC 1.6.5.3), (Gly) oxidation was lower than in the wild type and insensitive to rotenone, suggesting Complex I dysfunction. |
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| 11124957 | Grivennikova VG, Kapustin AN, Vinogradov AD: Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. evidence for the slow active/inactive transition. J Biol Chem. 2001 Mar 23;276(12):9038-44. Epub 2000 Dec 21. Alamethicin-treated mitochondria catalyzed the rotenone-sensitive -quinone reductase reaction with exogenousely added and -acceptor at the rates expected if the enzyme active sites would be freely accessible for the substrates. |
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| 17428841 | Koopman WJ, Verkaart S, Visch HJ, van Emst-de Vries S, Nijtmans LG, Smeitink JA, Willems PH: Human NADH:ubiquinone oxidoreductase deficiency: radical changes in mitochondrial morphology?. Am J Physiol Cell Physiol. 2007 Jul;293(1):C22-9. Epub 2007 Apr 11. |
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| 7957254 | Finel M, Majander AS, Tyynela J, De Jong AM, Albracht SP, Wikstrom M: Isolation and characterisation of subcomplexes of the mitochondrial NADH:ubiquinone oxidoreductase (complex I). Eur J Biochem. 1994 Nov 15;226(1):237-42. In addition, the Q-1 reductase activity of all the subcomplexes is insensitive to rotenone. |
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| 9593947 | Lummen P: Complex I inhibitors as insecticides and acaricides. Biochim Biophys Acta. 1998 May 6;1364(2):287-96. Structurally diverse synthetic insecticides and acaricides had been shown to inhibit the -translocating NADH:ubiquinone oxidoreductase (complex I) activity. Mechanistic studies indicated that these compounds interfered with reduction most likely at the same site (s) as the classical complex I inhibitors rotenone and piericidin A. |
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| 7607228 | Wisniewski E, Gellerich FN, Kunz WS: Distribution of flux control among the enzymes of mitochondrial oxidative phosphorylation in -activated saponin-skinned rat musculus soleus fibers. Eur J Biochem. 1995 Jun 1;230(2):549-54. The flux control coefficients of H (+)-ATPase, -nucleotide translocase, transporter, NADH:ubiquinone oxidoreductase and cytochrome-c oxidase were determined to be equal to 0.16 +/- 0.08 (n = 6), 0.34 +/- 0.12 (n = 5), 0.08 +/- 0.03 (n = 5), 0.01 +/- 0.006 (n = 4) and 0.09 +/- 0.03 (n = 3) using inhibitor titrations with the specific inhibitors oligomycin, carboxyatractyloside, mersalyl, rotenone and respectively, and applying non-linear regression of the entire titration curve. |
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| 14592541 | Tudella VG, Curti C, Soriani FM, Santos AC, Uyemura SA: In situ evidence of an alternative oxidase and an uncoupling protein in the respiratory chain of Aspergillus fumigatus. Int J Biochem Cell Biol. 2004 Jan;36(1):162-72. In addition, the ability of the fungus to oxidize exogenous as well as the insensitivity of its respiration to rotenone, in association with the sensitivity to indicate the presence of an alternative NADH-ubiquinone oxidoreductase; the partial sensitivity of respiration to antimycin A and in association with the sensitivity to benzohydroxamic acid, indicates the presence of an alternative oxidase. |
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| 12627969 | Peng G, Fritzsch G, Zickermann V, Schagger H, Mentele R, Lottspeich F, Bostina M, Radermacher M, Huber R, Stetter KO, Michel H: Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus. Biochemistry. 2003 Mar 18;42(10):3032-9. The A. aeolicus complex I is completely sensitive to rotenone and 2-n-decyl-quinazoline-4-yl-amine. |
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| 9915790 | Okun JG, Lummen P, Brandt U: Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase). J Biol Chem. 1999 Jan 29;274(5):2625-30. Although the rotenone site overlaps with both the piericidin A and the site, the latter two sites do not overlap. |
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| 19961238 | Shinzawa-Itoh K, Seiyama J, Terada H, Nakatsubo R, Naoki K, Nakashima Y, Yoshikawa S: Bovine heart NADH-ubiquinone oxidoreductase contains one molecule of with ten isoprene units as one of the cofactors. Biochemistry. 2010 Jan 26;49(3):487-92. The rotenone-sensitive enzymatic activity of the Complex I preparation was comparable to that of Complex I in the mitochondrial membrane. |
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| 2493147 | Ichiki T, Tanaka M, Kobayashi M, Sugiyama N, Suzuki H, Nishikimi M, Ohnishi T, Nonaka I, Wada Y, Ozawa T: Disproportionate deficiency of iron- clusters and subunits of complex I in mitochondrial encephalomyopathy. Pediatr Res. 1989 Feb;25(2):194-201. To investigate the molecular abnormality in the mitochondria from various tissues of an autopsied patient exhibiting mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes, we have examined the enzymatic activity, iron- cluster, and subunit composition of the NADH-ubiquinone oxidoreductase (complex I). Rotenone-sensitive -cytochrome c reductase activity was found to be decreased in all the tissues examined. |
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| 215122 | Ragan CI, Heron C: The interaction between mitochondrial NADH-ubiquinone oxidoreductase and -cytochrome c oxidoreductase. Biochem J. 1978 Sep 15;174(3):783-90. Experiments on the inhibition of the -cytochrome c oxidoreductase activity of mixtures of Complexes I and III by rotenone and antimycin indicate that electron transfer between a unit of Complex I-Complex III and extra molecules of Complexes I or III does not contribute to the overall rate of cytochrome c reduction. 3. |
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| 3134026 | Tanaka M, Nishikimi M, Suzuki H, Ozawa T, Ichiki T, Kobayashi M, Wada Y: Variation in the levels of complex I subunits among tissues in a patient with mitochondrial encephalomyopathy and renal dysfunction. Biochem Int. 1987 Apr;14(4):735-9. Enzymic activity and the levels of immunochemically detectable subunits of NADH-ubiquinone oxidoreductase (Complex I) were measured in the mitochondria from various tissues of a patient with mitochondrial encephalomyopathy and renal dysfunction. Rotenone-sensitive -cytochrome c reductase activity was decreased in all the tissues examined, but the degree of deficiency varied from tissue to tissue. |
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| 8627318 | Davey GP, Clark JB: Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria. J Neurochem. 1996 Apr;66(4):1617-24. Rotenone, myxothiazol, and KCN were used to titrate the activities of NADH:ubiquinone oxidoreductase (EC 1.6.5.3; complex I), ubiquinol:ferrocytochrome c oxidoreductase (EC 1.10.2.2; complex III), and cytochrome c oxidase (EC 1.9.3.1; complex IV ), respectively. |
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| 16342116 | Koopman WJ, Visch HJ, Smeitink JA, Willems PH: Simultaneous quantitative measurement and automated analysis of mitochondrial morphology, mass, potential, and motility in living human skin fibroblasts. Cytometry A. 2006 Jan;69(1):1-12. It was found that acute inhibition of mitochondrial complex I (NADH:ubiquinone oxidoreductase) by means of rotenone transiently reduced mitochondrial branching, area, and potential. |
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| 18797987 | Martins VP, Soriani FM, Magnani T, Tudella VG, Goldman GH, Curti C, Uyemura SA: Mitochondrial function in the yeast form of the pathogenic fungus Paracoccidioides brasiliensis. J Bioenerg Biomembr. 2008 Aug;40(4):297-305. Epub 2008 Sep 17. The presence of an alternative NADH-ubiquinone oxidoreductase was indicated by: (i) the ability to oxidize exogenous and (ii) the lack of sensitivity to rotenone and presence of sensitivity to |
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| 19220002 | King MS, Sharpley MS, Hirst J: Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (Complex I) and production of reactive species. Biochemistry. 2009 Mar 10;48(9):2053-62. Hydrophilic ubiquinones are reduced by an additional, non-energy-transducing pathway (which is insensitive to inhibitors such as rotenone and piericidin A). |
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| 8294484 | Herz U, Schroder W, Liddell A, Leaver CJ, Brennicke A, Grohmann L: Purification of the NADH:ubiquinone oxidoreductase (complex I) of the respiratory chain from the inner mitochondrial membrane of Solanum tuberosum. J Biol Chem. 1994 Jan 21;269(3):2263-9. The enzyme preparation showed an NADH:ubiquinone-2 reductase activity of 11.5 mumol x min-1 x mg-1 and is strongly inhibited by rotenone. |
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| 1332758 | Finel M, Skehel JM, Albracht SP, Fearnley IM, Walker JE: Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochemistry. 1992 Nov 24;31(46):11425-34. The line shapes of the EPR spectra of the Fe-S clusters are slightly broadened relative to spectra measured on complex I purified by conventional means, and the quinone reductase activity is insensitive to rotenone. |
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| 12556227 | Duarte M, Peters M, Schulte U, Videira A: The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria. Biochem J. 2003 May 1;371(Pt 3):1005-11. The 57 kDa NADH:ubiquinone oxidoreductase acts as internal (alternative) respiratory NADH dehydrogenase (NDI1) in the fungal mitochondria. The respiratory activity of mitochondria from the resulting null-mutant ndi1 is almost fully inhibited by rotenone, an inhibitor of the -pumping complex I, when matrix-generated is used as substrate. |
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| 215123 | Heron C, Ragan CI, Trumpower BL: The interaction between mitochondrial NADH-ubiquinone oxidoreductase and -cytochrome c oxidoreductase. Biochem J. 1978 Sep 15;174(3):791-800. |
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| 18353897 | Koopman WJ, Distelmaier F, Hink MA, Verkaart S, Wijers M, Fransen J, Smeitink JA, Willems PH: Inherited complex I deficiency is associated with faster protein diffusion in the matrix of moving mitochondria. Am J Physiol Cell Physiol. 2008 May;294(5):C1124-32. Epub 2008 Mar 19. We demonstrated previously that inhibition of mitochondrial complex I (CI or NADH:ubiquinone oxidoreductase) by rotenone accelerated matrix protein diffusion and decreased the fraction and velocity of moving mitochondria. |
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| 411483 | Crowder SE, Ragan CI: Effects of proteolytic digestion by chymotrypsin on the structure and catalytic properties of - oxidoreductase from bovine heart mitochondria. Biochem J. 1977 Aug 1;165(2):295-301. Incubation of NADH-ubiquinone oxidoreductase (Complex I) with chymotrypsin caused loss of rotenone-sensitive reduction and an increase in rotenone-insensitive reduction. 2. |
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| 1735444 | De Vries S, Van Witzenburg R, Grivell LA, Marres CA: Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur J Biochem. 1992 Feb 1;203(3):587-92. |
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| 17521330 | Cermakova P, Verner Z, Man P, Lukes J, Horvath A: Characterization of the NADH:ubiquinone oxidoreductase (complex I) in the trypanosomatid Phytomonas serpens (Kinetoplastida). FEBS J. 2007 Jun;274(12):3150-8. Epub 2007 May 22. Spectrophotometric measurement of the NADH:ubiquinone 10 and NADH:ferricyanide dehydrogenase activities revealed their different sensitivities to rotenone, piericidin, and diphenyl iodonium. |
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| 1445878 | Heinrich H, Werner S: Identification of the -binding site of NADH:ubiquinone oxidoreductase (complex I) from Neurospora crassa. Biochemistry. 1992 Nov 24;31(46):11413-9. The activity of the enzyme applying these derivatives is inhibited by 50% at a concentration of 9 and 20 microM rotenone. |
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| 12535666 | Chretien D, Benit P, Chol M, Lebon S, Rotig A, Munnich A, Rustin P: Assay of mitochondrial respiratory chain complex I in human lymphocytes and cultured skin fibroblasts. Biochem Biophys Res Commun. 2003 Jan 31;301(1):222-4. Respiratory chain complex I (NADH:ubiquinone oxidoreductase) deficiency is one of the most frequent causes of mitochondrial disease in humans. The procedure strongly reduces contaminating NADH:quinone oxidoreductase activity and permits measuring high rates of rotenone-sensitive complex I activity thanks to effective cell permeabilization. |
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| 2590688 | Sled' VD, Zinich VN, Kotliar AB: [One- and two-electron reduction of homologs by - dehydrogenase preparations from the mitochondrial respiratory chain]. Biokhimiia. 1989 Sep;54(9):1571-5. The mechanism of homologs reduction by different preparations of mitochondrial NADH dehydrogenase: complex I within submitochondrial particles, isolated NADH-ubiquinone oxidoreductase and soluble low molecular weight NADH dehydrogenase, has been investigated. It has been shown that oxidation via the rotenone-insensitive reaction is associated with one-electron reduction of low molecular weight homologs (Q0, Q1, Q2) to semiquinone with subsequent fast oxidation of the latter by atmospheric to form a |
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| 15262965 | Lambert AJ, Brand MD: Inhibitors of the -binding site allow rapid production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J Biol Chem. 2004 Sep 17;279(38):39414-20. Epub 2004 Jul 15. Despite complete inhibition of oxidoreductase activity in each case, different classes of -binding site inhibitor (rotenone, piericidin, and high concentrations of myxothiazol) gave different rates of production during forward electron transport (the rate with myxothiazol was twice that with rotenone) suggesting that the site of rapid generation by complex I is in the region of the -binding sites and not upstream at the flavin or low potential FeS centers. |
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| 9452319 | Blandini F, Nappi G, Greenamyre JT: Quantitative study of mitochondrial complex I in platelets of parkinsonian patients. Mov Disord. 1998 Jan;13(1):11-5. Activity of mitochondrial enzyme complex I (NADH-ubiquinone oxidoreductase) is reduced in the substantia nigra of patients with Parkinson's disease (PD). To obtain quantitative information on platelet complex I in PD, we studied platelet complex I in 16 PD patients and 16 age-matched controls by using a newly developed technique based on the binding of [3H] dihydrorotenone ([3H] DHR), an analog of the pesticide rotenone, to complex I. |
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| 18763029 | Zoccarato F, Cappellotto M, Alexandre A: Clorgyline and other propargylamine derivatives as inhibitors of -dependent H (2) O (2) release at NADH:UBIQUINONE oxidoreductase (Complex I) in brain mitochondria. J Bioenerg Biomembr. 2008 Aug;40(4):289-96. Epub 2008 Sep 2. O (2)(-) release is low with NAD-linked substrates and increases strongly during oxidation, which increases the QH (2)/Q ratio and is rotenone sensitive. |
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| 3020812 | Moore GA, O'Brien PJ, Orrenius S: -induced Ca2+ release from rat-liver mitochondria is caused by NAD (P) H oxidation. Xenobiotica. 1986 Sep;16(9):873-82. Incubation of rat-liver mitochondria with in the presence of and rotenone resulted in rapid and NAD (P) H oxidation followed by Ca2+ release and mitochondrial swelling. radical was formed by -resistant respiration, suggesting that undergoes a one-electron reduction to an autoxidizable semiquinone radical by NADH-ubiquinone oxidoreductase. |
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| 12231169 | Seo BB, Nakamaru-Ogiso E, Flotte TR, Yagi T, Matsuno-Yagi A: A single-subunit -quinone oxidoreductase renders resistance to mammalian nerve cells against complex I inhibition. Mol Ther. 2002 Sep;6(3):336-41. Numerous studies suggest that dysfunction of mitochondrial -translocating NADH-ubiquinone oxidoreductase (complex I) is associated with neurodegenerative disorders, such as Parkinson's disease and Huntington's disease. The cells expressing the Ndi1 protein were resistant to known inhibitors of complex I, such as rotenone and pyridaben. |
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| 8078526 | Beattie DS, Obungu VH, Kiaira JK: Oxidation of by a rotenone and antimycin-sensitive pathway in the mitochondrion of procyclic Trypanosoma brucei brucei. Mol Biochem Parasitol. 1994 Mar;64(1):87-94. We conclude that in the mitochondrion of the procyclic form of T. brucei, is preferentially oxidized by a rotenone-sensitive NADH:ubiquinone oxidoreductase; however, can also be oxidized to some extent by the enzyme reductase present in the mitochondrion of T. brucei. |
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| 14740892 | Pasdois P, Deveaud C, Voisin P, Bouchaud V, Rigoulet M, Beauvoit B: Contribution of the phosphorylable complex I in the growth phase-dependent respiration of C6 glioma cells in vitro. J Bioenerg Biomembr. 2003 Oct;35(5):439-50. Nevertheless, a quantitative correlation was found between cellular respiration and the rotenone-sensitive NADH ubiquinone oxidoreductase (i.e. complex I) activity. |
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| 12351220 | Helmerhorst EJ, Murphy MP, Troxler RF, Oppenheim FG: Characterization of the mitochondrial respiratory pathways in Candida albicans. Biochim Biophys Acta. 2002 Oct 3;1556(1):73-80. consumption by isolated mitochondria using or / as respiratory substrates indicated that C. albicans cells express both cytoplasmic and matrix NADH-ubiquinone oxidoreductase activities. In addition, / respiration was rotenone-sensitive, and an enzyme activity assay further confirmed that C. albicans cells express Complex I activity. |
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| 1907569 | Berger S, Ellersiek U, Steinmuller K: Cyanobacteria contain a mitochondrial complex I-homologous NADH-dehydrogenase. FEBS Lett. 1991 Jul 29;286(1-2):129-32. Both membranes oxidize in a rotenone-sensitive reaction. This demonstrates that a NADH-dehydrogenase, homologous to the mitochondrial NADH-ubiquinone-oxidoreductase (complex I of the respiratory chain) is present in cyanobacteria. |
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| 18485875 | Martinvalet D, Dykxhoorn DM, Ferrini R, Lieberman J: Granzyme A cleaves a mitochondrial complex I protein to initiate caspase-independent cell death. Cell. 2008 May 16;133(4):681-92. Here we find that GzmA accesses the mitochondrial matrix to cleave the complex I protein NDUFS3, an iron- subunit of the NADH:ubiquinone oxidoreductase complex I, after Lys56 to interfere with oxidation and generate anions. |
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| 9878531 | Li Y, Trush MA: Diphenyleneiodonium, an NAD (P) H oxidase inhibitor, also potently inhibits mitochondrial reactive species production. Biochem Biophys Res Commun. 1998 Dec 18;253(2):295-9. DPI was as potent as rotenone in inhibiting the production of and H2O2 by mitochondrial respiration. With substrate-supported isolated mitochondria, DPI was shown to reduce mitochondrial production probably through inhibiting NADH-ubiquinone oxidoreductase (complex I). |
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| 210762 | Ragan CI: The role of phospholipids in the reduction of analogues by the mitochondrial - oxidoreductase complex. Biochem J. 1978 Jun 15;172(3):539-47. The isolated NADH-ubiquinone oxidoreductase complex of bovine heart mitochondria reduces analogues by two pathways. One pathway is inhibited by rotenone, and reduction of quinones takes place in the lipid phase of the system. |
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| 8761491 | Buchanan SK, Walker JE: Large-scale chromatographic purification of F1F0-ATPase and complex I from bovine heart mitochondria. Biochem J. 1996 Aug 15;318 ( Pt 1):343-9. The complex I preparation contains all of the subunits identified in other preparations of the enzyme, and has rotenone-sensitive NADH:ubiquinone oxidoreductase and NADH:ferricyanide oxidoreductase activities. |
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| 17463293 | Tanaka-Esposito C, Chen Q, Moghaddas S, Lesnefsky EJ: Ischemic preconditioning does not protect via blockade of electron transport. J Appl Physiol. 2007 Aug;103(2):623-8. Epub 2007 Apr 26. Maximally expressed complex I activity measured as rotenone-sensitive NADH:ubiquinone oxidoreductase in detergent-solubilized mitochondria was also unaffected by IPC. |
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| 11454754 | Remacle C, Baurain D, Cardol P, Matagne RF: Mutants of Chlamydomonas reinhardtii deficient in mitochondrial complex I: characterization of two mutations affecting the nd1 coding sequence. Genetics. 2001 Jul;158(3):1051-60. The mitochondrial rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) comprises more than 30 subunits, the majority of which are encoded by the nucleus. |
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| 9030267 | Glinn MA, Lee CP, Ernster L: Pro- and anti-oxidant activities of the mitochondrial respiratory chain: factors influencing NAD (P) H-induced lipid peroxidation. Biochim Biophys Acta. 1997 Jan 16;1318(1-2):246-54. This paper is a study of factors influencing the rate of lipid peroxidation in beef heart submitochondrial particles induced by NAD (P) H via the NADH-ubiquinone oxidoreductase (Complex I) of the respiratory chain. Rotenone did not eliminate the biphasicity of the -induced reaction, indicating that this was not due to an antioxidant effect of at high concentrations. |
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| 20074573 | Nakamaru-Ogiso E, Han H, Matsuno-Yagi A, Keinan E, Sinha SC, Yagi T, Ohnishi T: The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor. FEBS Lett. 2010 Mar 5;584(5):883-8. Epub 2010 Jan 13. NADH:ubiquinone oxidoreductase (complex I) is the entry enzyme of mitochondrial oxidative phosphorylation. The cross-linking was blocked by rotenone. |
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| 10433094 | Myers MA, Georgiou HM, Byron S, Esposti MD: Inhibition of mitochondrial oxidative phosphorylation induces hyper-expression of glutamic acid decarboxylase in pancreatic islet cells. Autoimmunity. 1999;30(1):43-51. Inhibitors of NADH-ubiquinone oxidoreductase (complex I) seem to be particularly effective in increasing the expression of GAD in both foetal mouse pancreas and HIT-T15 hamster beta cells, especially in the presence of nutrients such as and |
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| 9878712 | Ushakova AV, Grivennikova VG, Ohnishi T, Vinogradov AD: Triton X-100 as a specific inhibitor of the mammalian NADH-ubiquinone oxidoreductase (Complex I). Biochim Biophys Acta. 1999 Jan 5;1409(3):143-53. Triton X-100 inhibits the oxidase and rotenone-sensitive -Q1 reductase activities of bovine heart submitochondrial particles (SMP) with an apparent Ki of 1x10-5 M (pH 8.0, 25 degrees C). |
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| 16402917 | Reinecke F, Levanets O, Olivier Y, Louw R, Semete B, Grobler A, Hidalgo J, Smeitink J, Olckers A, Van der Westhuizen FH: Metallothionein isoform 2A expression is inducible and protects against ROS-mediated cell death in rotenone-treated HeLa cells. Biochem J. 2006 Apr 15;395(2):405-15. The role of MT (metallothionein) gene expression was investigated in rotenone-treated HeLa cells to induce a deficiency of NADH:ubiquinone oxidoreductase (complex I). |
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| 12079358 | Cardol P, Matagne RF, Remacle C: Impact of mutations affecting ND mitochondria-encoded subunits on the activity and assembly of complex I in Chlamydomonas. J Mol Biol. 2002 Jun 21;319(5):1211-21. The mitochondrial rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) comprises more than 35 subunits, the majority of which are encoded by the nucleus. |
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| 16410242 | Schonfeld P, Reiser G: Rotenone-like action of the branched-chain induces oxidative stress in mitochondria. J Biol Chem. 2006 Mar 17;281(11):7136-42. Epub 2006 Jan 12. The interference of Phyt with the electron transport was demonstrated by inhibition of state 3- and p-trifluoromethoxyphenylhydrazone (FCCP)-dependent respiration, inactivation of the NADH-ubiquinone oxidoreductase complex in permeabilized mitochondria, decrease in reduction of the synthetic electron acceptor 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium in state 4, and increase of the mitochondrial NAD (P) H level in FCCP-uncoupled mitochondria. |
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| 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. J Neurochem. 2000 Dec;75(6):2611-21. In vivo [(3) H] DHR binding was markedly reduced by local and systemic infusion of rotenone and was enhanced by local administration. |
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| 8312726 | Yamada K, Fukushima T: Mechanism of cytotoxicity of paraquat. Exp Toxicol Pathol. 1993 Oct;45(5-6):375-80. Paraquat also stimulated O2- production in bovine liver NADH-ubiquinone oxidoreductase (complex I). O2- production was stimulated by paraquat even in the presence of rotenone, one of the mitochondrial respiratory chain inhibitors. |
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| 1463844 | Ellersiek U, Steinmuller K: Cloning and transcription analysis of the ndh (A-I-G-E) gene cluster and the ndhD gene of the cyanobacterium Synechocystis sp. Plant Mol Biol. 1992 Dec;20(6):1097-110. The plastid DNA of higher plants contains eleven reading frames that are homologous to subunits of the mitochondrial NADH-ubiquinone oxidoreductase (complex I). The enzyme is sensitive to rotenone and is located on the cytoplasmic and the thylakoid membrane. |
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| 10652103 | Steuber J, Schmid C, Rufibach M, Dimroth P: Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli. Mol Microbiol. 2000 Jan;35(2):428-34. Following on from our previous discovery of Na+ pumping by the NADH:ubiquinone oxidoreductase (complex I) of Klebsiella pneumoniae, we show here that complex I from Escherichia coli is a Na+ pump as well. The transport activity of vesicles from /-grown cells was 40 nmol mg-1 min-1 and was resistant to the uncoupler carbonyl- m-chlorophenylhydrazone (CCCP), but was inhibited by the complex I-specific inhibitor rotenone. |
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| 10433118 | Combettes B, Grienenberger JM: Analysis of wheat mitochondrial complex I purified by a one-step immunoaffinity chromatography. Biochimie. 1999 Jun;81(6):645-53. In order to isolate the mitochondrial respiratory chain complex I (NADH:ubiquinone oxidoreductase EC 1.6.99.3) from wheat, we developed a one-step immunoaffinity procedure using antibodies raised against the NAD9 subunit. The complex retained on the column proved to be a functional complex I, since the preparation showed NADH:duroquinone and NADH:FeK3 (CN) 6 reductase activities which were inhibited by rotenone. |
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| 3132077 | Ichiki T, Tanaka M, Nishikimi M, Suzuki H, Ozawa T, Kobayashi M, Wada Y: Deficiency of subunits of Complex I and mitochondrial encephalomyopathy. . Ann Neurol. 1988 Mar;23(3):287-94. Enzymic activities of the respiratory chain and content of immunochemically detectable subunits in NADH-ubiquinone oxidoreductase (Complex I) were measured in mitochondria from the skeletal muscles of 4 patients with mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes (MELAS). The rotenone-sensitive -cytochrome c reductase activity was extremely decreased, ranging from 0% to 27% of the control value. |
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| 16963630 | Cardol P, Lapaille M, Minet P, Franck F, Matagne RF, Remacle C: ND3 and ND4L subunits of mitochondrial complex I, both nucleus encoded in Chlamydomonas reinhardtii, are required for activity and assembly of the enzyme. Eukaryot Cell. 2006 Sep;5(9):1460-7. Made of more than 40 subunits, the rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) is the most intricate membrane-bound enzyme of the mitochondrial respiratory chain. |
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| 8192914 | Birch-Machin MA, Briggs HL, Saborido AA, Bindoff LA, Turnbull DM: An evaluation of the measurement of the activities of complexes I-IV in the respiratory chain of human skeletal muscle mitochondria. Biochem Med Metab Biol. 1994 Feb;51(1):35-42. Complex I activity is measured in the presence of 2.5 mg.ml-1 bovine serum albumin, which increases rotenone sensitivity, and we have shown that NADH-cytochrome b5 reductase makes an important contribution to the rotenone-insensitive NADH-ubiquinone oxidoreductase activity. |
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| 11695186 | Schuler F, Casida JE: The insecticide target in the PSST subunit of complex I. . Pest Manag Sci. 2001 Oct;57(10):932-40. This process has often ended up with compounds of high potency as inhibitors of the electron transport chain and more specifically of complex I (NADH:ubiquinone oxidoreductase). |
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| 18781777 | Ichimaru N, Murai M, Kakutani N, Kako J, Ishihara A, Nakagawa Y, Nishioka T, Yagi T, Miyoshi H: Synthesis and characterization of new piperazine-type inhibitors for mitochondrial NADH-ubiquinone oxidoreductase (complex I). Biochemistry. 2008 Oct 7;47(40):10816-26. Epub 2008 Sep 10. The mode of action of Deltalac-acetogenins, strong inhibitors of bovine heart mitochondrial complex I, is different from that of traditional inhibitors such as rotenone and piericidin A [Murai, M., et al. (2007) Biochemistry 46 , 6409-6416]. |
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| 8026508 | De Jong AM, Albracht SP: Ubisemiquinones as obligatory intermediates in the electron transfer from to Eur J Biochem. 1994 Jun 15;222(3):975-82. Until now ubisemiquinones associated with NADH:ubiquinone oxidoreductase (complex I) have been reported to occur in isolated enzyme and in tightly coupled submitochondrial particles. The EPR signal of the rotenone-sensitive ubisemiquinones could be detected not only in coupled MgATP submitochondrial particles, but also in routine preparations of uncoupled submitochondrial particles and in mitochondria. |
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| 16214040 | Garait B, Couturier K, Servais S, Letexier D, Perrin D, Batandier C, Rouanet JL, Sibille B, Rey B, Leverve X, Favier R: Fat intake reverses the beneficial effects of low caloric intake on skeletal muscle mitochondrial H (2) O (2) production. Free Radic Biol Med. 2005 Nov 1;39(9):1249-61. Epub 2005 Aug 8. H (2) O (2) production was significantly reduced in Lou/C rats fed a HC diet; this effect was not due to a lower O (2) consumption but rather to a decrease in rotenone-sensitive NADH-ubiquinone oxidoreductase activity and increased expression of uncoupling proteins 2 and 3. |
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