| Name | NADH dehydrogenase |
|---|---|
| Synonyms | B14.5b; NADH dehydrogenase; CI B14.5b; Complex I B14.5b; HLC 2; HLC2; NADH dehydrogenase [ubiquinone] 1 subunit C2; NADH ubiquinone oxidoreductase subunit B14.5b… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2350337 | Krueger MJ, Singer TP, Casida JE, Ramsay RR: Evidence that the blockade of mitochondrial respiration by the neurotoxin 1-methyl-4-phenylpyridinium (MPP+) involves binding at the same site as the respiratory inhibitor, rotenone. Biochem Biophys Res Commun. 1990 May 31;169(1):123-8. It has been postulated that 1-methyl-4-phenylpyridinium (MPP+) blocks mitochondrial respiration by combining at the same site as rotenone, a potent inhibitor of oxidation in mitochondria, known to act at the junction of NADH dehydrogenase and |
81(1,1,1,1) | Details |
| 1751550 | Gregory RB, Berry MN: On the thyroid hormone-induced increase in respiratory capacity of isolated rat hepatocytes. Biochim Biophys Acta. 1991 Dec 3;1098(1):61-7. However, less rotenone was required for maximal inhibition of respiration in the hypothyroid state than in cells from euthyroid or hyperthyroid rats, implying that hepatocytes from hypothyroid animals contain less NADH dehydrogenase. |
81(1,1,1,1) | Details |
| 8981035 | Rao DN, Cederbaum AI: A comparative study of the redox-cycling of a (rifamycin S) and a quinonimine (rifabutin) antibiotic by rat liver microsomes. Free Radic Biol Med. 1997;22(3):439-46. The electron transport chain inhibitors such as rotenone and antimycin A enhanced the signal intensity of DMPO-OH, suggesting NADH dehydrogenase (complex I) as the major component involved in the reduction of rifamycin S. |
31(0,1,1,1) | Details |
| 17127363 | Gomez C, Bandez MJ, Navarro A: Pesticides and impairment of mitochondrial function in relation with the parkinsonian syndrome. Front Biosci. 2007 Jan 1;12:1079-93. Toxicants that inhibit selectively NADH-dehydrogenase activity, as rotenone or pyridaben, also show a selective inhibition of O2 uptake and respiratory control in rat brain mitochondria in the presence of NAD-dependent substrates. |
31(0,1,1,1) | Details |
| 9893134 | Heitzer T, Wenzel U, Hink U, Krollner D, Skatchkov M, Stahl RA, MacHarzina R, Brasen JH, Meinertz T, Munzel T: Increased NAD (P) H oxidase-mediated production in renovascular hypertension: evidence for an involvement of protein kinase C. Kidney Int. 1999 Jan;55(1):252-60. Vascular O-.2 was normalized by the PKC inhibitor calphostin C, by the inhibitor of flavin-dependent oxidases, diphenylene iodonium, and recombinant -binding superoxide dismutase, whereas inhibitors of the xanthine oxidase synthase (NG-nitro- and mitochondrial NADH dehydrogenase (rotenone) were ineffective. |
31(0,1,1,1) | Details |
| 2919886 | Cino M, Del Maestro RF: Generation of peroxide by brain mitochondria: the effect of reoxygenation following postdecapitative ischemia. Arch Biochem Biophys. 1989 Mar;269(2):623-38. -supported H2O2 generation was diminished by rotenone and the uncoupler carbonyl m-chlorphenylhydrazone and enhanced by antimycin A and increased tensions. When maximally reduced, the NADH dehydrogenase and the -cytochrome b regions of the electron transport chain are sources of H2O2. |
2(0,0,0,2) | Details |
| 16668549 | Luethy MH, Hayes MK, Elthon TE: Partial Purification and Characterization of Three NAD (P) H Dehydrogenases from Beta vulgaris Mitochondria. Plant Physiol. 1991 Dec;97(4):1317-1322. Mitochondria isolated from the taproot of beet (Beta vulgaris) were used in an effort to identify and partially purify the proteins constituting the exogenous NADH dehydrogenase. All three peaks are insensitive to divalent cation chelators and a complex I inhibitor, rotenone. |
2(0,0,0,2) | Details |
| 16344601 | French SW: The pathogenesis and significance of the urinary cycle in rats fed intragastrically. Alcohol Clin Exp Res. 2005 Nov;29(11 Suppl):158S-161S. When complex I (NADH dehydrogenase) of the mitochondrial electron transport chain is inhibited by feeding rotenone, the cycle is totally eliminated and blood levels remain constant at 200 mg/%. |
81(1,1,1,1) | Details |
| 7797053 | Gusev GP, Sherstobitov AO: Effect of metabolic inhibitors on K+ transport across the lamprey (Lampetra fluviatilis) erythrocyte membrane. Gen Physiol Biophys. 1994 Dec;13(6):459-68. It may be suggested that NADH dehydrogenase is the key enzyme required for active transport of K+ in the cells, as rotenone, a selective blocker of this enzyme, causes a complete blockade of the Na+, K (+)-pump. |
81(1,1,1,1) | Details |
| 16667685 | Pascal N, Dumas R, Douce R: Comparison of the Kinetic Behavior toward Nucleotides of -Linked Dehydrogenases from Plant Mitochondria. Plant Physiol. 1990 Sep;94(1):189-193. It is suggested that (+)-linked malic enzyme, when fully activated, is able to raise the matricial level up to the required concentration to fully engage the rotenone-resistant internal NADH-dehydrogenase, whose affinity for is weaker than complex I. |
31(0,1,1,1) | Details |
| 6461651 | Di Virgilio F, Azzone GF: Activation of site I redox-driven H+ pump by exogenous quinones in intact mitochondria. J Biol Chem. 1982 Apr 25;257(8):4106-13. The data support the view that the NADH dehydrogenase possesses two redox sites, one accounting for the rotenone-sensitive reduction and another accounting for the rotenone-insensitive reduction. |
31(0,1,1,1) | Details |
| 17055488 | Seo BB, Marella M, Yagi T, Matsuno-Yagi A: The single subunit NADH dehydrogenase reduces generation of reactive species from complex I. FEBS Lett. 2006 Nov 13;580(26):6105-8. Epub 2006 Oct 16. Incubation of non-transduced cells with rotenone elicited oxidative damage to mitochondrial DNA as well as lipid peroxidation. |
2(0,0,0,2) | Details |
| 7561883 | Sabri MI, Lystrup B, Roy DN, Spencer PS: Action of beta-N-oxalylamino- on mouse brain NADH-dehydrogenase activity. J Neurochem. 1995 Oct;65(4):1842-8. Two known inhibitors (rotenone and 1-methyl-4-phenylpyridinium ion, MPP+) of this mitochondrial enzyme produced significant inhibition under identical conditions. |
2(0,0,0,2) | Details |
| 8397143 | Adams JD Jr, Klaidman LK, Leung AC: MPP+ and MPDP+ induced radical formation with mitochondrial enzymes. Free Radic Biol Med. 1993 Aug;15(2):181-6. MPP+ has been reported to inhibit (NADH) dehydrogenase in mitochondria, which results in the formation of O2 (.-). MPP+ may be capable of interacting with submitochondrial particles at a site other than the rotenone site, which results in some formation of radicals. |
2(0,0,0,2) | Details |
| 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. The kinetics of this decrease correlated with solubilization of the low-molecular-weight type-II NADH dehydrogenase (subunit mol.wts. 53000 and 27000) and with degradation of a polypeptide of mol.wt. 30000. 6. |
2(0,0,0,2) | Details |
| 3707593 | Ferreira J, Wilkinson C, Gil L: The locus of inhibition of oxidation by benzothiadiazoles in beef heart submitochondrial particles. Biochem Int. 1986 Mar;12(3):447-59. The data suggest that 6-Cl-BTD interacts with an electron transport site on the side of NADH dehydrogenase and inhibitory studies with 6-Cl-BTD and rotenone indicate that it might correspond with one of the two sites affected by rotenone. |
81(1,1,1,1) | Details |
| 14972026 | Johansson FI, Michalecka AM, Moller IM, Rasmusson AG: Oxidation and reduction of nucleotides in alamethicin-permeabilized plant mitochondria. Biochem J. 2004 May 15;380(Pt 1):193-202. AlaM was found to inhibit the electron-transport chain at the external Ca2+-dependent rotenone-insensitive NADH dehydrogenase and around complexes III and IV. |
81(1,1,1,1) | Details |
| 8512585 | Lund BO, Miller DM, Woods JS: Studies on Hg (II)-induced H2O2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria. Biochem Pharmacol. 1993 May 25;45(10):2017-24. This effect was accompanied by significantly increased H2O2 formation, GSH depletion and TBARS formation linked to both NADH dehydrogenase (rotenone-inhibited) and -cytochrome b (antimycin-inhibited) regions of the electron transport chain. |
31(0,1,1,1) | Details |
| 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. Both NADH:cytochrome c and NADH:ubiquinone reductase activities were inhibited 80-90% by rotenone indicating the presence of a complex I-like NADH dehydrogenase in the mitochondrion of trypanosomes. |
31(0,1,1,1) | Details |
| 6293697 | Doroshow JH: Effect of anthracycline antibiotics on radical formation in rat heart. Cancer Res. 1983 Feb;43(2):460-72. Doxorubicin stimulated mitochondrial formation in a dose-dependent manner that also appeared to follow saturation kinetics (apparent Km of 454.55 microM); however, drug-related production by mitochondria required rather than and was significantly increased in the presence of rotenone, which suggested that the proximal portion of the mitochondrial NADH dehydrogenase complex [NADH:(acceptor) oxidoreductase, EC 1.6.99.3] was responsible for the reduction of doxorubicin at this site. |
31(0,1,1,1) | Details |
| 9404058 | Sue M, Miyoshi H, Iwamura H: Specific interaction of cytokinins and their analogs with rotenone-sensitive internal NADH dehydrogenase in potato tuber mitochondria. Biosci Biotechnol Biochem. 1997 Nov;61(11):1806-9. |
31(0,1,1,1) | Details |
| 4303099 | Bois R, Estabrook RW: Nonheme iron protein as a possible site of rotenone inhibition of mitochondrial NADH dehydrogenase. Arch Biochem Biophys. 1969 Jan;129(1):362-9. |
81(1,1,1,1) | Details |
| 15526465 | Sharova IV, Vekshin NL: [Rotenone-insensitive oxydation in mitochondrial suspension occurs by NADH dehydrogenase of respiratory chain fragments]. Biofizika. 2004 Sep-Oct;49(5):814-21. The oxidation of the added by mitochondria in hypotonic media occurs only through the NADH dehydrogenase of the respiratory chain, since it was totally blocked by rotenone or amytal (and also by antimycin A or azide), but the ferricyanide-activated oxidation was insensitive to these inhibitors. |
69(0,2,3,4) | 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. 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. |
31(0,1,1,1) | Details |
| 6713449 | Quinn PJ, Crutcher EC: The action of beta-adrenoceptor antagonists on rat heart mitochondrial function in vitro: a comparison of timolol, and Cardiovasc Res. 1984 Apr;18(4):212-9. Transfer of electrons through Complex I measured by the rate of reduction of ferricyanide by submitochondrial particles inhibited by rotenone and the lack of specific inhibition by of supported respiration indicated that one site of drug action was between NADH dehydrogenase and its associated flavoprotein, possibly close to the site of rotenone inhibition. |
31(0,1,1,1) | Details |
| 198640 | Sokolov GV, Eremina SS, Lozinov AB: [Respiratory chain of Candida mycoderma] . Mikrobiologiia. 1977 Jul-Aug;46(4):597-604. At the exponential growth phase, only the first pathway of electron transport, including rotenone-resistant NADH-dehydrogenase, functions. |
31(0,1,1,1) | Details |
| 11863445 | Fang J, Beattie DS: Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization. Biochemistry. 2002 Mar 5;41(9):3065-72. |
14(0,0,2,4) | Details |
| 7941733 | Buschges R, Bahrenberg G, Zimmermann M, Wolf K: oxidoreductase in obligate aerobic yeasts. Yeast. 1994 Apr;10(4):475-9. In S. cerevisiae, a rotenone-insensitive NADH dehydrogenase of about 500-600 kDa is detected only in stationary phase cells. |
12(0,0,2,2) | Details |
| 3110216 | Hoppel CL, Kerr DS, Dahms B, Roessmann U: Deficiency of the dehydrogenase component of complex I of mitochondrial electron transport. J Clin Invest. 1987 Jul;80(1):71-7. Mitochondrial NADH dehydrogenase activity (complex I, assayed as rotenone-sensitive oxidase, -duroquinone reductase, and -cytochrome c reductase) was 0-10% of controls, and -ferricyanide reductase activity was 25-50% of controls in the mitochondria and in skin fibroblasts. |
12(0,0,2,2) | Details |
| 8833408 | Matsunaga T, Kudo J, Takahashi K, Dohmen K, Hayashida K, Okamura S, Ishibashi H, Niho Y: Rotenone, a mitochondrial NADH dehydrogenase inhibitor, induces cell surface expression of CD13 and CD38 and apoptosis in HL-60 cells. Leuk Lymphoma. 1996 Feb;20(5-6):487-94. |
63(0,2,2,3) | Details |
| 12270629 | Fang J, Beattie DS: Rotenone-insensitive NADH dehydrogenase is a potential source of in procyclic Trypanosoma brucei mitochondria. Mol Biochem Parasitol. 2002 Aug 28;123(2):135-42. These results suggest that the rotenone-insensitive NADH dehydrogenase in addition to reductase is a potential source of production in procyclic trypanosome mitochondria. |
43(0,1,3,3) | Details |
| 16661455 | Rustin P, Moreau F, Lance C: Oxidation in Plant Mitochondria via Malic Enzyme and the -insensitive Electron Transport Pathway. Plant Physiol. 1980 Sep;66(3):457-462. It is concluded that malic enzyme and a specific pool of NAD (+)/ are connected to the -insensitive alternative pathway by a specific rotenone-insensitive NADH dehydrogenase located on the inner face of the inner membrane. |
12(0,0,2,2) | Details |
| 10844979 | Obungu VH, Kiaira JK, Olembo NK, Njogu MR: Pathways of catabolism in procyclic Trypanosoma congolense. Indian J Biochem Biophys. 1999 Oct;36(5):305-11. Studies of respiration on in procyclic Trypanosoma congolense in the presence of rotenone, antimycin, salicylhydroxamic acid and have indicated the presence of NADH dehydrogenase, cytochrome b-c1, cytochrome aa3, trypanosome alternate oxidase and reductase/succinate dehydrogenase pathway that contributes electrons to of the respiratory chain. |
12(0,0,2,2) | Details |
| 4315616 | Gutman M, Singer TP, Beinert H, Casida JE: Reaction sites of rotenone, piericidin A, and amytal in relation to the nonheme iron components of NADH dehydrogenase. Proc Natl Acad Sci U S A. 1970 Mar;65(3):763-70. |
8(0,0,1,3) | Details |
| 6745260 | Cook ND, Cammack R: Purification and characterization of the rotenone-insensitive NADH dehydrogenase of mitochondria from Arum maculatum. Eur J Biochem. 1984 Jun 15;141(3):573-7. Affinity chromatography on 5'-ADP-Sepharose 4B was used to separate the rotenone-sensitive (complex I) NADH dehydrogenase from the rotenone-insensitive NADH dehydrogenase. |
43(0,1,3,3) | Details |
| 6625611 | Walker GH, Oliver DJ: Changes in the electron transport chain of pea leaf mitochondria metabolizing Arch Biochem Biophys. 1983 Sep;225(2):847-53. At higher concentrations the rotenone-insensitive NADH dehydrogenase was increasingly important and its increased electron transport capacity was best exploited by malate dehydrogenase. |
38(0,1,2,3) | Details |
| 3168972 | Dechecchi MC, Girella E, Cabrini G, Berton G: The Km of NADH dehydrogenase is decreased in mitochondria of cystic fibrosis cells. Enzyme. 1988;40(1):45-50. The kinetic properties of the NADH dehydrogenase of the mitochondrial respiratory chain, assayed as -dependent rotenone-sensitive cytochrome c reductase have been studied in mitochondria isolated from mononuclear white blood cells in patients affected by cystic fibrosis. |
7(0,0,1,2) | Details |
| 15140267 | Geisler DA, Johansson FI, Svensson AS, Rasmusson AG: Antimycin A treatment decreases respiratory internal rotenone-insensitive oxidation capacity in potato leaves. BMC Plant Biol. 2004 May 12;4:8. RESULTS: We report a specific decrease in internal rotenone-insensitive NADH dehydrogenase capacity in mitochondria from antimycin A-treated leaves. |
7(0,0,1,2) | Details |
| 823748 | Schewe T, Hiebsch C, Halangk W: [Action of the systemic fungicide dexon on several NADH dehydrogenases] . Acta Biol Med Ger. 1975;34(11-12):1767-75. Furthermore, dexon inhibits the NADH dehydrogenase located at the outer surface of the inner membrane of plant mitochondria, accessible to extramitochondrial and insensitive to rotenone, as has been shown on isolated mitochondria from cauliflower (Brassica oleracea L). |
33(0,1,1,3) | Details |
| 3691507 | Nohl H: Demonstration of the existence of an organo-specific NADH dehydrogenase in heart mitochondria. Eur J Biochem. 1987 Dec 15;169(3):585-91. The "exogenous NADH dehydrogenase" of heart mitochondria was found to introduce reducing equivalents into the respiratory chain before the rotenone block, indicating that the enzyme is associated with complex I. |
32(0,1,1,2) | Details |
| 3178753 | Cottingham IR, Moore AL: Analysis of NADH dehydrogenases from plant [mung bean (Phaseolus aureus)] mitochondrial membranes on non-denaturing polyacrylamide gels and purification of complex I by band excision. Biochem J. 1988 Aug 15;254(1):303-5. A rotenone-sensitive NADH dehydrogenase (Complex I) was identified on the basis of co-migration with the purified mammalian enzyme. |
7(0,0,1,2) | Details |
| 12615344 | Bandeiras TM, Salgueiro CA, Huber H, Gomes CM, Teixeira M: The respiratory chain of the thermophilic archaeon Sulfolobus metallicus: studies on the type-II NADH dehydrogenase. Biochim Biophys Acta. 2003 Mar 6;1557(1-3):13-9. The membranes of the thermoacidophilic archaeon Sulfolobus metallicus exhibit an consumption activity of 0.5 nmol O (2) min (-1) mg (-1), which is insensitive to rotenone, suggesting the presence of a type-II NADH dehydrogenase. |
7(0,0,1,2) | Details |
| 19747108 | Torrentino-Madamet M, Desplans J, Travaille C, James Y, Parzy D: Microaerophilic Respiratory Metabolism of Plasmodium falciparum Mitochondrion as a Drug Target. Curr Mol Med. 2009 Sep 13. In addition, we provide details on certain characteristics like the lack of pyruvate dehydrogenase, the existence of a rotenone-insensitive NADH-dehydrogenase, the possible existence of an alternative oxidase, and uncoupled proteins. |
6(0,0,1,1) | Details |
| 11971654 | Krungkrai J, Kanchanarithisak R, Krungkrai SR, Rochanakij S: Mitochondrial NADH dehydrogenase from Plasmodium falciparum and Plasmodium berghei. Exp Parasitol. 2002 Jan;100(1):54-61. NADH dehydrogenase of respiratory complex I was demonstrated in isolated mitochondrial organelles of the human parasite Plasmodium falciparum and the mouse parasite Plasmodium berghei by using the specific inhibitor rotenone on consumption and enzyme activity. |
32(0,1,1,2) | Details |
| 20205678 | Torrentino-Madamet M, Desplans J, Travaille C, James Y, Parzy D: Microaerophilic respiratory metabolism of Plasmodium falciparum mitochondrion as a drug target. Curr Mol Med. 2010 Feb 1;10(1):29-46. In addition, we provide details on certain characteristics like the lack of pyruvate dehydrogenase, the existence of a rotenone-insensitive NADH-dehydrogenase, the possible existence of an alternative oxidase, and uncoupled proteins. |
6(0,0,1,1) | Details |
| 8798503 | Menz RI, Day DA: Purification and characterization of a 43-kDa rotenone-insensitive NADH dehydrogenase from plant mitochondria. J Biol Chem. 1996 Sep 20;271(38):23117-20. |
6(0,0,1,1) | Details |
| 11479321 | Bai Y, Hajek P, Chomyn A, Chan E, Seo BB, Matsuno-Yagi A, Yagi T, Attardi G: Lack of complex I activity in human cells carrying a mutation in MtDNA-encoded ND4 subunit is corrected by the Saccharomyces cerevisiae -quinone oxidoreductase (NDI1) gene. J Biol Chem. 2001 Oct 19;276(42):38808-13. Epub 2001 Jul 30. The gene for the single subunit, rotenone-insensitive, and -sensitive internal -quinone oxidoreductase of Saccharomyces cerevisiae (NDI1) can completely restore the NADH dehydrogenase activity in mutant human cells that lack the essential mitochondrial DNA (mtDNA)-encoded subunit ND4. |
6(0,0,1,1) | Details |
| 6263247 | Turrens JF, Boveris A: Generation of by the NADH dehydrogenase of bovine heart mitochondria. Biochem J. 1980 Nov 1;191(2):421-7. Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of and rotenone or by reversed electron transfer generate 0.9 +/- 0.1 nmol of O2-/min per mg of protein at pH 7.4 and at 30 degrees C. |
164(2,2,2,4) | Details |
| 6409169 | Galkina VG, Iaguzhinskii LS: [Action of strong and weak nitrogenous bases on respiratory chain enzymes of mitochondria]. Nauchnye Doki Vyss Shkoly Biol Nauki. 1983;(5):12-7. The nitrogenous basis with a long alkoxylic group is shown to be inhibitors of NADH-dehydrogenase, their action is similar to rotenone. |
32(0,1,1,2) | Details |
| 3790070 | Cottingham IR, Cleeter MW, Ragan CI, Moore AL: Immunological analysis of plant mitochondrial NADH dehydrogenases. . Biochem J. 1986 May 15;236(1):201-7. The other approach was to probe plant mitochondrial membranes with antibodies raised to a purified preparation of ox heart rotenone-sensitive NADH dehydrogenase and subunits thereof. |
6(0,0,1,1) | Details |
| 8075112 | Singer TP, Ramsay RR: The reaction sites of rotenone and with mitochondrial NADH dehydrogenase. Biochim Biophys Acta. 1994 Aug 30;1187(2):198-202. |
6(0,0,1,1) | Details |
| 1239310 | Yaguzhinski LS, Kolesova GM: [Model of bifunctional binding of rotenone and piericidin with mitochondrial NADH-dehydrogenase]. Biokhimiia. 1975 May-Jun;40(3):456-60. |
162(2,2,2,2) | Details |
| 8944779 | Beattie DS, Howton MM: The presence of rotenone-sensitive NADH dehydrogenase in the long slender bloodstream and the procyclic forms of Trypanosoma brucei brucei. Eur J Biochem. 1996 Nov 1;241(3):888-94. Low levels of rotenone-sensitive -dependent reduction of dichloroindophenol and the presence of subunits 7 and 8 of NADH dehydrogenase provided additional evidence for the presence of NADH dehydrogenase in bloodstream forms of T. brucei. |
119(1,2,3,4) | Details |
| 12763610 | Fonck C, Baudry M: Rapid reduction of ATP synthesis and lack of free radical formation by MPP+ in rat brain synaptosomes and mitochondria. Brain Res. 2003 Jun 13;975(1-2):214-21. For comparison, the respiratory toxins FCCP, a analog that uncouples mitochondrial ATP production, and rotenone, a NADH dehydrogenase inhibitor, were also tested. |
31(0,1,1,1) | Details |
| 12226375 | Moller IM, Roberts TH, Rasmusson AG: Induces External Deamino- Oxidation in Potato Tuber Mitochondria. Plant Physiol. 1996 Sep;112(1):75-78. We conclude that UQ-1-induced external deamino- oxidation is due to a change in specificity of the external rotenone-insensitive NADH dehydrogenase. |
31(0,1,1,1) | Details |
| 2561442 | Stephenson G, Sanadi DR: Evidence that coupling factor B is bound to the matrix side of the inner mitochondrial membrane. Biochem Int. 1989 Nov;19(5):1087-94. Rotenone-sensitive NADH dehydrogenase activity and Lubrol stimulation of cytochrome oxidase activity were measured to assess the opposite membrane polarity of beef heart mitoplast and inside-out particle preparations. |
6(0,0,1,1) | Details |
| 18197244 | Marella M, Seo BB, Nakamaru-Ogiso E, Greenamyre JT, Matsuno-Yagi A, Yagi T: Protection by the NDI1 gene against neurodegeneration in a rotenone rat model of Parkinson's disease. PLoS One. 2008 Jan 16;3(1):e1433. Using the rotenone rat model, we investigated the protective effects of alternative NADH dehydrogenase (Ndi1) which we previously demonstrated to act as a replacement for complex I both in vitro and in vivo. |
6(0,0,1,1) | Details |
| 17196160 | Yamamoto F, Ohgari Y, Yamaki N, Kitajima S, Shimokawa O, Matsui H, Taketani S: The role of in (ALA)-induced photosensitivity of cancerous cells. Biochem Biophys Res Commun. 2007 Feb 16;353(3):541-6. Epub 2006 Dec 22. The levels of mitochondrial ferrochelatase and rotenone-sensitive NADH dehydrogenase in the NOS2-induced cells decreased. |
6(0,0,1,1) | Details |
| 786986 | Dancey GF, Levine AE, Shapiro BM: The NADH dehydrogenase of the respiratory chain of Escherichia coli. J Biol Chem. 1976 Oct 10;251(19):5911-20. The NADH dehydrogenase of the Escherichia coli respiratory chain has been identified by the following properties: (a) its location in membrane vesicles; (b) its inhibition by AMP in a fashion similar to that of the oxidase; (c) its specificity for but not with the same Km for as that of the oxidase; (d) its sensitivity when membrane-bound to inhibition by dicoumarol, rotenone, and 2-heptyl-4-hydroxyquinoline-N-oxide, which are also inhibitors for the oxidase. |
3(0,0,0,3) | Details |
| 2002336 | Ramsay RR, Krueger MJ, Youngster SK, Gluck MR, Casida JE, Singer TP: Interaction of 1-methyl-4-phenylpyridinium ion (MPP+) and its analogs with the rotenone/piericidin binding site of NADH dehydrogenase. J Neurochem. 1991 Apr;56(4):1184-90. |
112(1,2,2,2) | Details |
| 6819864 | Palmer JM, Schwitzguebel JP, Moller IM: Regulation of oxidation in plant mitochondria. Biochem J. 1982 Dec 15;208(3):703-11. It is therefore concluded that added NAD+ gains access to the matrix space and stimulates oxidation by the rotenone-resistant NADH dehydrogenase located on the matrix surface of the inner membrane. |
112(1,2,2,2) | Details |
| 37504 | Shapiro BL, Feigal RJ, Lam LF: Mitrochondrial NADH dehydrogenase in cystic fibrosis. . Proc Natl Acad Sci U S A. 1979 Jun;76(6):2979-83. Because rotenone specifically inhibits NADH dehydrogenase, (acceptor) oxidoreductase, EC 1.6.99.3], which is the enzyme of energy-conserving site 1 of the mitochondrial electron transport system, activity and kinetics of this enzyme system were studied in fibroblast homogenates. |
84(1,1,1,4) | Details |
| 7180843 | Shapiro BL, Lam LF, Feigal RJ: Mitochondrial NADH dehydrogenase in cystic fibrosis: enzyme kinetics in cultured fibroblasts. Am J Hum Genet. 1982 Nov;34(6):846-52. Differences among cystic fibrosis (CF) genotypes (CF, obligate carriers for CF [HZ], and controls) in mitochondrial pool size, (O2) consumption, and rotenone inhibition of O2 consumption led to examination of mitochondrial NADH dehydrogenase [acceptor] oxidoreductase, E.C. 1.6.99.3). pH optima of mitochondrial NADH dehydrogenase were different in enzyme derived from whole cell homogenates of cultured skin fibroblasts of subjects with CF, HZ, and controls. |
83(1,1,1,3) | Details |
| 1768276 | Lund BO, Miller DM, Woods JS: Mercury-induced H2O2 production and lipid peroxidation in vitro in rat kidney mitochondria. Biochem Pharmacol. 1991 Dec 11;42 Suppl:S181-7. In mitochondria supplemented with a respiratory chain substrate or / and an electron transport inhibitor (antimycin A (AA) or rotenone), Hg (II) (30 nmol/mg protein) increased H2O2 formation approximately 4-fold at the -cytochrome b region (AA-inhibited) and 2-fold at the NADH dehydrogenase region (rotenone-inhibited). |
82(1,1,1,2) | 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 -cytochrome c reductase to antimycin is indicative of the absence of the classical complex I of the electron transfer chain in this bacterium. |
31(0,1,1,1) | Details |
| 15032834 | Hagedorn PH, Flyvbjerg H, Moller IM: Modelling turnover in plant mitochondria. . Physiol Plant. 2004 Mar;120(3):370-385. It is produced by enzymes in, or associated with, the tricarboxylic acid cycle in the matrix, and it is oxidized by two respiratory chain enzymes in the inner membrane, the rotenone-sensitive complex I and the rotenone-insensitive internal NADH dehydrogenase (ND (in)). |
31(0,1,1,1) | Details |
| 16662684 | Moreau F, Romani R: Oxidation and -Insensitive Respiration in Avocado Mitochondria during the Climacteric Cycle. Plant Physiol. 1982 Nov;70(5):1385-1390. It appears that a functional connection exists between malic enzyme and the alternative pathway via a rotenone-insensitive NADH dehydrogenase and that this pathway is responsible, in part, for nonphosphorylating respiratory activity during the climacteric. |
6(0,0,1,1) | Details |
| 14645467 | Sherer TB, Betarbet R, Testa CM, Seo BB, Richardson JR, Kim JH, Miller GW, Yagi T, Matsuno-Yagi A, Greenamyre JT: Mechanism of toxicity in rotenone models of Parkinson's disease. J Neurosci. 2003 Nov 26;23(34):10756-64. To determine the molecular site of action of rotenone, cells were transfected with the rotenone-insensitive single-subunit NADH dehydrogenase of Saccharomyces cerevisiae (NDI1), which incorporates into the mammalian ETC and acts as a "replacement" for endogenous complex I. |
6(0,0,1,1) | 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. Complex I inhibitors like rotenone and annonine were inactive, clearly excluding the presence of a coupled NADH dehydrogenase. |
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| 6245637 | Ingledew WJ, Ohnishi T: An analysis of some thermodynamic properties of iron- centres in site I of mitochondria. Biochem J. 1980 Jan 15;186(1):111-7. Oxidation-reduction titrations of iron- centres with the couple /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 5. |
83(1,1,1,3) | Details |
| 16663348 | Chauveau M, Dizengremel P, Roussaux J: Interaction of Benzylaminopurine with Electron Transport in Plant Mitochondria during Oxidation. Plant Physiol. 1983 Dec;73(4):945-948. A pH of 7.7 favored the activity of malate dehydrogenase, which is connected with a rotenone-sensitive NADH dehydrogenase, whereas at pH 6.5 malic enzyme, linked to a rotenone-resistant NADH dehydrogenase, was more active.Experimental results indicate the existence of two sites of inhibition for BA. |
31(0,1,1,1) | Details |
| 8648915 | Zager RA: Mitochondrial free radical production induces lipid peroxidation during myohemoglobinuria. Kidney Int. 1996 Mar;49(3):741-51. Site 2 (antimycin A) or site 3 hypoxia) mitochondrial respiratory chain inhibition completely blocked lipid peroxidation, whereas site 1 inhibition (rotenone) doubled its extent (presumably by shunting through NADH dehydrogenase, a free radical generating system). |
31(0,1,1,1) | 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. |
6(0,0,1,1) | Details |
| 7707312 | Andreani A, Rambaldi M, Leoni A, Locatelli A, Ghelli A, Ratta M, Benelli B, Degli Esposti M: Thienylimidazo [2,1-b] thiazoles as inhibitors of mitochondrial NADH dehydrogenase. J Med Chem. 1995 Mar 31;38(7):1090-7. This compound is noncompetitive with the substrate and interacts with a site which is mutually exclusive with that of rotenone but nonexclusive with that of piericidin and several other inhibitors of NADH dehydrogenase. |
83(1,1,1,3) | Details |
| 1991043 | Ramsay RR, Krueger MJ, Youngster SK, Singer TP: Evidence that the inhibition sites of the amine 1-methyl-4-phenylpyridinium (MPP+) and of the respiratory chain inhibitor piericidin A are the same. Biochem J. 1991 Jan 15;273(Pt 2):481-4. 1-Methyl-4-phenylpyridinium (MPP+), the bioactivation product of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), interrupts mitochondrial electron transfer at the NADH dehydrogenase- junction, as do the respiratory chain inhibitors rotenone, piericidin A and barbiturates. |
82(1,1,1,2) | Details |
| 19508504 | Rustin P, Jacobs HT: Respiratory chain alternative enzymes as tools to better understand and counteract respiratory chain deficiencies in human cells and animals. Physiol Plant. 2009 Dec;137(4):362-70. Epub 2009 May 6. These alternative enzymes, e.g. the -insensitive alternative oxidase and the internal rotenone-insensitive NADH dehydrogenase, confer a significant flexibility to the respiratory chain, allowing it to overcome potential constraints exerted by the cell phosphorylation potential or by environmental xenobiotics. |
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| 16662949 | Boydston R, Paxton JD, Koeppe DE: Glyceollin: A Site-Specific Inhibitor of Electron Transport in Isolated Soybean Mitochondria. Plant Physiol. 1983 May;72(1):151-155. The glyceollin inhibition of electron transport by isolated soybean and corn mitochondria was similar to that of rotenone, acting at site I between the internal NADH dehydrogenase and |
31(0,1,1,1) | Details |
| 6536673 | Landi L, Pasquali P, Cabrini L, Sechi AM, Lenaz G: On the mechanism of inhibition of oxidase by -3. J Bioenerg Biomembr. 1984 Apr;16(2):153-66. The combined effects of rotenone and -3 on the kinetics of NADH dehydrogenase and oxidase have been investigated. |
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| 12566073 | Fang J, Beattie DS: External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of Free Radic Biol Med. 2003 Feb 15;34(4):478-88. Three rotenone-insensitive NADH dehydrogenases are present in the mitochondria of yeast Saccharomyces cerevisiae, which lack complex I. |
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| 9707444 | Bai Y, Attardi G: The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme. EMBO J. 1998 Aug 17;17(16):4848-58. |
3(0,0,0,3) | Details |
| 16668682 | Soole KL, Dry IB, Wiskich JT: Partial Purification and Characterization of Complex I, NADH:Ubiquinone Reductase, from the Inner Membrane of Beetroot Mitochondria. Plant Physiol. 1992 Feb;98(2):588-594. A NADH dehydrogenase was isolated from an inner membrane-enriched fraction of beetroot mitochondria (Beta vulgaris L.) by solubilization with and purified using gel filtration and affinity chromatography. The purified NADH dehydrogenase complex catalyzed the reduction of various electron acceptors with as the electron donor, was not sensitive to rotenone inhibition, and had a slow - reductase activity. |
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| 7774132 | Takeshige K: formation and lipid peroxidation by the mitochondrial electron-transfer chain]. Rinsho Shinkeigaku. 1994 Dec;34(12):1269-71. Electrons from are supplied to the reactions from a component between the substrate site and the rotenone-sensitive site of the NADH dehydrogenase. |
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| 14561532 | Tada-Oikawa S, Hiraku Y, Kawanishi M, Kawanishi S: Mechanism for generation of peroxide and change of mitochondrial membrane potential during rotenone-induced apoptosis. Life Sci. 2003 Nov 7;73(25):3277-88. These results suggest that rotenone induces O2 (-)-derived H2O2 generation through inhibition of NADH dehydrogenase complex and/or activation of NAD (P) H oxidase, and H2O2 generation causes the disruption of mitochondrial membrane in rotenone-induced apoptosis. |
82(1,1,1,2) | Details |
| 9878636 | Duby F, Matagne RF: Alteration of dark respiration and reduction of phototrophic growth in a mitochondrial DNA deletion mutant of Chlamydomonas lacking cob, nd4, and the 3' end of nd5. Plant Cell. 1999 Jan;11(1):115-25. The low respiratory rate of the dum24 cells results from the activities of rotenone-resistant NADH dehydrogenase, complex II, and alternative oxidase, with none of these enzymes being coupled to ATP production. |
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| 8135820 | Pecci L, Montefoschi G, Fontana M, Cavallini D: Aminoethylcysteine ketimine decarboxylated dimer inhibits mitochondrial respiration by impairing electron transport at complex I level. Biochem Biophys Res Commun. 1994 Mar 15;199(2):755-60. These results give a preliminary indication suggesting that the dimer inhibits electron flow from NADH dehydrogenase to at or near the rotenone binding site (s). |
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| 7775420 | Gonzalez-Flecha B, Demple B: Metabolic sources of peroxide in aerobically growing Escherichia coli. J Biol Chem. 1995 Jun 9;270(23):13681-7. Compounds that block electron transport at NADH dehydrogenase (rotenone) or between and cytochrome b (antimycin) showed that univalent reduction of O2 can occur at these sites in vivo to form (O2-), in agreement with reports for mammalian mitochondria. |
31(0,1,1,1) | Details |
| 3456345 | Davies KJ, Doroshow JH: Redox cycling of anthracyclines by cardiac mitochondria. J Biol Chem. 1986 Mar 5;261(7):3060-7. Anthracycline radical formation by NADH dehydrogenase.. Inhibitor experiments (rotenone, amytal, piericidin A) indicated that the anthracycline reduction site lies on the substrate side of |
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| 7823960 | Hofhaus G, Attardi G: Efficient selection and characterization of mutants of a human cell line which are defective in mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase. Mol Cell Biol. 1995 Feb;15(2):964-74. In the course of analysis of eight mutants of the human cell line VA2B selected for their resistance to high concentrations of the complex I inhibitor rotenone, seven were found to be respiration deficient, and among these, six exhibited a specific defect of complex I. |
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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. |
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| 6786284 | Takeshige K, Takayanagi R, Minakami S: Lipid peroxidation and the reduction of ADP-Fe3+ chelate by -ubiquinone reductase preparation from bovine heart mitochondria. Biochem J. 1980 Dec 15;192(3):861-6. These observations suggest that electrons from reduced coenzymes are transferred to ADP-Fe3+ chelate from a component between a mercurial-sensitive site and the rotenone-sensitive one of the NADH dehydrogenase and that the reduction of ADP-Fe3+ chelate by the NADH dehydrogenase is an essential step in the lipid peroxidation. |
81(1,1,1,1) | Details |
| 1722151 | Rasmusson AG, Moller IM: Effect of ions and inhibitors on internal NAD (P) H dehydrogenases in plant mitochondria. Eur J Biochem. 1991 Dec 5;202(2):617-23. Mersalyl and dicumarol, two potent inhibitors of the external NADH dehydrogenase in plant mitochondria, were found to inhibit internal rotenone-insensitive NAD (P) H oxidation, at the same concentrations and in manners very similar to their effects on the external NAD (P) H oxidation. |
81(1,1,1,1) | Details |
| 10491287 | Mills KI, Woodgate LJ, Gilkes AF, Walsh V, Sweeney MC, Brown G, Burnett AK: Inhibition of mitochondrial function in HL60 cells is associated with an increased apoptosis and expression of CD14. Biochem Biophys Res Commun. 1999 Sep 24;263(2):294-300. The potential of mitochondrial inhibitors to induce differentiation was investigated by treating the HL60 cells with either the NADH dehydrogenase inhibitor, Rotenone, the complex III inhibitor, Antimycin A, or the highly specific mitochondrial ATP-synthase inhibitor, Oligomycin. |
31(0,1,1,1) | Details |
| 8403080 | Snyder JW, Alexander GM, Ferraro TN, Grothusen JR, Farber JL: N-methyl-4-phenylpyridinium (MPP+) potentiates the killing of cultured hepatocytes by catecholamines. Chem Biol Interact. 1993 Sep;88(2-3):209-23. The toxicity of catecholamines was also potentiated by the mitochondrial site I (NADH dehydrogenase) inhibitor rotenone. |
31(0,1,1,1) | Details |
| 2249975 | Dreyer JL: Plasma membrane dehydrogenases in rat brain synaptic membranes. J Bioenerg Biomembr. 1990 Oct;22(5):619-33. The supernatant retained over 60% of the NADH-dehydrogenase activity, tested with either DCIP2 or ferricyanide as substrates, together with Both enzyme activities were insensitive toward rotenone. |
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| 3941077 | Nisimoto Y, Wilson E, Heyl BL, Lambeth JD: NADH dehydrogenase from bovine neutrophil membranes. J Biol Chem. 1986 Jan 5;261(1):285-90. No effects were seen with mitochondrial respiratory inhibitors such as azide, or rotenone, but p-chloromercuribenzoate was strongly inhibitory and N-ethylmaleimide was weakly inhibitory. |
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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 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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| 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 (MTT), suggesting a deficiency in NADH dehydrogenase and/or succinate dehydrogenase activities. |
81(1,1,1,1) | Details |
| 16662080 | Johnson-Flanagan AM, Spencer MS: The Effect of Rotenone on Respiration in Pea Cotyledon Mitochondria. . Plant Physiol. 1981 Dec;68(6):1211-1217. Rotenone also inhibited the NADH dehydrogenase associated with malate dehydrogenase. |
81(1,1,1,1) | Details |
| 39543 | Takeshige K, Minakami S: - and -dependent formation of anions by bovine heart submitochondrial particles and -ubiquinone reductase preparation. Biochem J. 1979 Apr 15;180(1):129-35. These findings suggest that a region between a mercurialsensitive site and the rotenone-sensitive site of the respiratory-chain NADH dehydrogenase is largely responsible for the - and -dependent O (2) (-) production by the mitochondrial inner membranes. |
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| 10413091 | Cook-Johnson RJ, Zhang Q, Wiskich JT, Soole KL: The nuclear origin of the non-phosphorylating NADH dehydrogenases of plant mitochondria. FEBS Lett. 1999 Jul 2;454(1-2):37-41. Based on these results we have concluded that the matrix facing rotenone-insensitive NADH dehydrogenase of plant mitochondria is encoded by a nuclear gene and synthesis of the protein occurs in the cytosol. |
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| 8377005 | Krueger MJ, Sablin SO, Ramsay R, Singer TP: Reactivation of NADH dehydrogenase (complex I) inhibited by 1-methyl-4-(4'-alkylphenyl) pyridinium analogues: a clue to the nature of the inhibition site. J Neurochem. 1993 Oct;61(4):1546-8. MPP+ and its analogues have been shown to block electron transport at or near the same site as two powerful inhibitors of mitochondrial respiration, rotenone and piericidin A. |
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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. The NADH dehydrogenase is synthesized as a precursor protein containing a signal sequence of 26 residues. |
3(0,0,0,3) | Details |
| 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. Cyanobacteria also contain a NADH dehydrogenase that is homologous to the mitochondrial complex I. The enzyme is sensitive to rotenone and is located on the cytoplasmic and the thylakoid membrane. |
3(0,0,0,3) | Details |
| 14634020 | Zoccarato F, Cavallini L, Alexandre A: Respiration-dependent removal of exogenous H2O2 in brain mitochondria: inhibition by Ca2+. J Biol Chem. 2004 Feb 6;279(6):4166-74. Epub 2003 Nov 20. This appears to depend on -supported production of H2O2 by reverse electron flow at NADH dehydrogenase competing with exogenous H2O2 for removal. -dependent H2O2 is inhibited by rotenone, decreased DeltaPsi, as described previously, and by ruthenium red and / |
1(0,0,0,1) | Details |
| 6495407 | Petrenko AIu, Belous AM, Zhegunov GF: [Ca2+ release from rat liver mitochondria subjected to deep freezing] . Ukr Biokhim Zh. 1984 Jul-Aug;56(4):447-51. ATPase and NADH-dehydrogenase inhibitors when introduced into the medium simultaneously with mitochondria prevent the both processes, but only till Ca2+ release. |
1(0,0,0,1) | Details |
| 1737983 | Basma AN, Heikkila RE, Saporito MS, Philbert M, Geller HM, Nicklas WJ: 1-Methyl-4-(2'-ethylphenyl)-1,2,3,6-tetrahydropyridine-induced toxicity in PC12 cells is enhanced by preventing glycolysis. J Neurochem. 1992 Mar;58(3):1052-9. The effects of 1-methyl-4-(2'-ethylphenyl)-1,2,3,6-tetrahydropyridine (2'Et-MPTP), 1-methyl-4-(2'-ethylphenyl) pyridinium (2'Et-MPP+), and the classic complex 1 inhibitor, rotenone, on toxicity as well as on rates of use and lactate production were studied using the pheochromocytoma PC12 cell line. PC12 cells are neoplastic in nature and have a high rate of glycolysis accompanied by a large production of lactate and a low use of carbon through the Krebs cycle. 1-Methyl-4-phenylpyridinium (MPP+) and analogues such as 2'Et-MPP+ are actively accumulated by mitochondrial preparations in vitro and block NADH dehydrogenase of complex 1. |
1(0,0,0,1) | Details |
| 6298008 | Davies KJ, Doroshow JH, Hochstein P: Mitochondrial NADH dehydrogenase-catalyzed radical production by adriamycin, and the relative inactivity of 5-iminodaunorubicin. FEBS Lett. 1983 Mar 7;153(1):227-30. |
1(0,0,0,1) | Details |
| 12468742 | Karpova OV, Kuzmin EV, Elthon TE, Newton KJ: Differential expression of alternative oxidase genes in maize mitochondrial mutants. Plant Cell. 2002 Dec;14(12):3271-84. The expression pattern is specific for each type of mitochondrial lesion: the NADH dehydrogenase-defective NCS2 mutant has high expression of aox2, whereas the cytochrome oxidase-defective NCS6 mutant predominantly expresses aox3. |
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| 4155266 | de Otamendi ME, Stoppani AO: Action of diethylstilbestrol on the NADH-dehydrogenase region of the respiratory chain. Arch Biochem Biophys. 1974 Nov;165(1):21-33. |
1(0,0,0,1) | Details |
| 18786503 | Lin SS, Kerscher S, Saleh A, Brandt U, Gross U, Bohne W: The Toxoplasma gondii type-II NADH dehydrogenase TgNDH2-I is inhibited by 1--2-alkyl-4 (1H) quinolones. Biochim Biophys Acta. 2008 Nov;1777(11):1455-62. Epub 2008 Aug 22. The apicomplexan parasite Toxoplasma gondii does not possess complex I of the mitochondrial respiratory chain, but has two genes encoding rotenone-insensitive, non- pumping type-II NADH dehydrogenases (NDH2s). |
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| 18551278 | Lin PC, Puhar A, Steuber J: oxidation drives respiratory Na+ transport in mitochondria from Yarrowia lipolytica. Arch Microbiol. 2008 Oct;190(4):471-80. Epub 2008 Jun 13. By purification and reconstitution into proteoliposomes, a respiratory NADH dehydrogenase was identified which coupled -dependent reduction of (1.4 micromol min (-1) mg (-1)) to Na+ translocation (2.0 micromol min (-1) mg (-1)). -driven Na+ transport was sensitive towards rotenone, a specific inhibitor of complex I. |
1(0,0,0,1) | Details |
| 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 An increase in activity and gene expression of the alternative NADH dehydrogenase throughout the yeast's exponential growth phase was observed. |
1(0,0,0,1) | Details |
| 15763667 | Mariano AB, Valente C, Cadena SM, Rocha ME, de Oliveira MB, Carnieri EG: Sensitivities of the alternative respiratory components of potato tuber mitochondria to thiol reagents and Ca2+. Plant Physiol Biochem. 2005 Jan;43(1):61-7. Another feature of plant mitochondria is that besides complex I (EC 1.6.5.3) they possess alternative NAD (P) H-dehydrogenases insensitive to rotenone. In the present study we investigated the effects of some thiol reagents and Ca (2+) on potato mitochondrial respiratory chain presenting different activities of the alternative respiratory components AOX and external NADH dehydrogenase, a condition induced by previous treatment of potato tubers (Solanum tuberosum L., cv. |
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| 2253761 | Singer TP, Ramsay RR: Mechanism of the neurotoxicity of MPTP. FEBS Lett. 1990 Nov 12;274(1-2):1-8. Recent experiments suggest that the binding site is at or near the combining site of the classical respiratory inhibitors, rotenone and piericidin A. Following concentration in the neurons by the synaptic system, which has a high affinity for the carrier, MPP+ and its positively charged analogs are further concentrated by the electrical gradient of the inner membrane and then more slowly penetrate the hydrophobic reaction site on NADH dehydrogenase. |
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| 9270009 | Gerhauser C, Lee SK, Kosmeder JW, Moriarty RM, Hamel E, Mehta RG, Moon RC, Pezzuto JM: Regulation of ornithine decarboxylase induction by deguelin, a natural product cancer chemopreventive agent. Cancer Res. 1997 Aug 15;57(16):3429-35. These results suggest that antimicrotubule effects, as mediated by rotenone, for example, are not responsible for inhibitory activity facilitated by deguelin. As anticipated, however, NADH dehydrogenase was inhibited by these rotenoids. |
1(0,0,0,1) | Details |
| 16041863 | Gills JJ, Kosmeder J 2nd, Moon RC, Lantvit DD, Pezzuto JM: Effect of deguelin on UVB-induced skin carcinogenesis. . J Chemother. 2005 Jun;17(3):297-301. These results are of interest as they contradict a major hypothesis for the mode of action of deguelin, i.e., a general down regulation of signal transduction based on inhibition of NADH dehydrogenase and depletion of ATP levels. |
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| 11551316 | Lyddiard JR, Whitfield PJ: Inhibition of Site I mitochondrial electron transport by an extract of the seeds of Millettia thonningii: a potential mechanism for the plant's molluscicidal and schistosome larvicidal activity. J Helminthol. 2001 Sep;75(3):259-65. The extract was found to inhibit mitochondrial electron transport at Site I (NADH dehydrogenase) at concentrations of 30-159 mg x l (-1). Although the extract is not as potent an inhibitor at Site I as rotenone, a known inhibitor of NADH dehydrogenase, such observations could explain the molluscicidal and schistosomicidal activity of dichloromethane extracts of the seeds of M. thonningii. |
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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. We have previously shown that the single-subunit NADH dehydrogenase of Saccharomyces cerevisiae (Ndi1P) can work as a replacement for complex I in mammalian cells. The cells expressing the Ndi1 protein were resistant to known inhibitors of complex I, such as rotenone and pyridaben. |
1(0,0,0,1) | Details |
| 7727510 | Gonzalez-Flecha B, Boveris A: Mitochondrial sites of peroxide production in reperfused rat kidney cortex. Biochim Biophys Acta. 1995 Apr 13;1243(3):361-6. Electron transport and production of O2-/H2O2 by the NADH dehydrogenase flavin-semiquinone and (UQH.) were studied in a model of in vivo ischemia-reperfusion in rat kidney. H2O2 production rates were assessed in isolated mitochondria using either with and without antimycin, or - with and without rotenone. |
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| 11695833 | Yagi T, Seo BB, Di Bernardo S, Nakamaru-Ogiso E, Kao MC, Matsuno-Yagi A: NADH dehydrogenases: from basic science to biomedicine. J Bioenerg Biomembr. 2001 Jun;33(3):233-42. This review article is concerned with two on-going research projects in our laboratory, both of which are related to the study of the NADH dehydrogenase enzyme complexes in the respiratory chain. This project involves attempting to repair complex I defects in the mammalian system using Saccharomyces cerevisiae NDI1 genes, which code for the internal, rotenone-insensitive -quinone oxidoreductase. |
2(0,0,0,2) | Details |
| 8619621 | Schonheit K, Nohl H: Oxidation of cytosolic via complex I of heart mitochondria. . Arch Biochem Biophys. 1996 Mar 15;327(2):319-23. The exogenous NADH dehydrogenase of heart mitochondria is increasingly reported to mediate cardiomyopathies following adriamycin treatment or reperfusion of ischemic hearts. Our studies exclude both the rotenone-insensitive NADH dehydrogenase of the outer membrane and the endogenous NADH dehydrogenase of damaged mitochondria as being responsible for external consumption. |
2(0,0,0,2) | Details |
| 3297786 | Earley FG, Patel SD, Ragan I, Attardi G: Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [3H] dihydrorotenone. FEBS Lett. 1987 Jul 13;219(1):108-12. |
2(0,0,0,2) | Details |
| 7654209 | Grivell AR, Korpelainen EI, Williams CJ, Berry MN: Substrate-dependent utilization of the or / redox shuttles by Ehrlich ascites cells. Biochem J. 1995 Sep 1;310 ( Pt 2):665-71. Rotenone, an inhibitor of NADH dehydrogenase, and amino-oxyacetate, which inhibits the / shuttle, were powerful suppressors of reducing equivalent flux from lactate as sole substrate, but were much less potent in the presence of carbohydrate. Rotenone, an inhibitor of NADH dehydrogenase, and amino-oxyacetate, which inhibits the / shuttle, were powerful suppressors of reducing equivalent flux from lactate as sole substrate, but were much less potent in the presence of carbohydrate. |
1(0,0,0,1) | Details |
| 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 |
1(0,0,0,1) | Details |
| 6317663 | Kang D, Narabayashi H, Sata T, Takeshige K: Kinetics of formation by respiratory chain - dehydrogenase of bovine heart mitochondria. J Biochem. 1983 Oct;94(4):1301-6. Formation of anions (O2-) by bovine heart NADH-dehydrogenase preparation (Complex I) supported by an - or -generating system was studied kinetically. The plots of the -dependent activity of rotenone-treated submitochondrial particles were also biphasic. |
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| 4310792 | Albracht SP, Slater EC: Reconstitutively active NADH dehydrogenase. Biochim Biophys Acta. 1969 Oct 21;189(2):308-10. |
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| 11804876 | Matecki S, Py G, Lambert K, Peyreigne C, Mercier J, Prefaut C, Ramonatxo M: Effect of prolonged undernutrition on rat diaphragm mitochondrial respiration. Am J Respir Cell Mol Biol. 2002 Feb;26(2):239-45. With plus rotenone, there was no significant difference in the respiratory rate between groups. In the ND group, we found a significant decrease in citrate synthase activity (P < 0.01), and also in reduced nicotinamine dinucleotide (NADH) dehydrogenase activity (P < 0.05), which cannot alone induce such a state 3 respiratory decrease. |
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| 2421769 | Malviya AN, Mandel P, Mersel M: The nature of DT-diaphorase (EC 1.6.99.2) activity in plasma membrane of astrocytes in primary cultures. Biochim Biophys Acta. 1986 Apr 24;849(2):288-92. DT-diaphorase-type activity is also observed on the cell surface employing dichloroindophenol as external electron acceptor and it is found to be a dicoumarol-sensitive NADH dehydrogenase. |
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| 7190438 | Mackler B, Haynes B, Person R, Palmer G: Electron transport systems of Candida utilis: purification and properties of the respiratory chain-linked external NADH dehydrogenase. Biochim Biophys Acta. 1980 Jul 8;591(2):289-97. Rotenone (10 (-5) M) and seconal (10 (-3) M) do not inhibit enzymatic activity. |
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| 11370674 | Velazquez I, Pardo JP: Kinetic characterization of the rotenone-insensitive internal oxidoreductase of mitochondria from Saccharomyces cerevisiae. Arch Biochem Biophys. 2001 May 1;389(1):7-14. Saccharomyces cerevisiae mitochondria contain an NADH:Q6 oxidoreductase (internal NADH dehydrogenase) encoded by NDI1 gene in chromosome XIII. |
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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. NADH dehydrogenase activity was characterized in the mitochondrial lysates of Phytomonas serpens, a trypanosomatid flagellate parasitizing plants. 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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| 2995124 | Tarakhovsky AM, Umansky VJ, Shlyakhovenko VA, Balitsky KP: Redox-dependent activation of 5'-nucleotidase in rat liver plasma membranes. FEBS Lett. 1985 Sep 23;189(2):338-40. -dependent activation of 5'-nucleotidase was significantly suppressed by atebrine, an inhibitor of NADH dehydrogenase of plasma membranes, and completely abolished by 2,4-dinitrophenol (2 X 10 (-4) M) and Triton X-100 (2%). Inhibitors of electron transfer in the mitochondrial respiratory chain, rotenone and failed to affect 5'-nucleotidase activity in both the presence and absence of |
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| 947364 | Harmon HJ, Crane FL: Inhibition of mitochondrial electron transport by hydrophilic metal chelators. Biochim Biophys Acta. 1976 Jul 9;440(1):45-58. Inter-complex electron flow is prevented by rotenone or thenoyltrifluoroacetone. Inhibiton by hydrophilic chelators only in mitochondria indicates that succinate dehydrogenase as well as NADH dehydrogenase has a transmembranous orientation. |
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| 8662757 | Hofhaus G, Johns DR, Hurko O, Attardi G, Chomyn A: Respiration and growth defects in transmitochondrial cell lines carrying the 11778 mutation associated with Leber's hereditary optic neuropathy. J Biol Chem. 1996 May 31;271(22):13155-61. However, NADH dehydrogenase-dependent respiration, as measured in digitonin-permeabilized cells, was specifically decreased by approximately 40% in cells carrying the mutation. On the contrary, no decrease in rotenone-sensitive NADH dehydrogenase activity, using a water-soluble analogue as electron acceptor, was detected in disrupted mitochondrial membranes. |
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| 17855661 | Hsu YC, Lee HC, Ping YH, Liu TY, Lui WY, Chi CW: Mitochondria are an essential mediator of /cyclic 3',5'-monophosphate blocking of depletion induced cytotoxicity in human HepG2 cells. Mol Cancer Res. 2007 Sep;5(9):923-32. Furthermore, we found that rotenone and antimycin A (mitochondria complex I and III inhibitors, respectively) blocked SNP cytoprotection against depletion-induced cytotoxicity. Moreover, depletion decreased the expression of various mitochondrial proteins, including cytochrome c, complex I (NADH dehydrogenase), complex III (cytochrome c reductase), and heat shock protein 60; these depletion-induced effects were blocked by SNP. |
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| 1645458 | Bienen EJ, Saric M, Pollakis G, Grady RW, Clarkson AB Jr: Mitochondrial development in Trypanosoma brucei brucei transitional bloodstream forms. Mol Biochem Parasitol. 1991 Apr;45(2):185-92. The EMF is inhibited by 2,4-dinitrophenol, rotenone and salicylhydroxamic acid but not by antimycin A or Consequently, NADH dehydrogenase, site I of oxidative phosphorylation, is the source of the EMF and the plant-like trypanosome alternative oxidase (TAO) supports the electron flow serving as the terminal oxidase of the chain. |
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| 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. |
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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. The results described in this report lead to the conclusion that ubisemiquinones form obligatory intermediates in the reaction of NADH dehydrogenase with 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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| 16659616 | Day DA, Rayner JR, Wiskich JT: Characteristics of External Oxidation by Beetroot Mitochondria. . Plant Physiol. 1976 Jul;58(1):38-42. These mitochondria have a rotenone- and antimycin-insensitive pathway of oxidation associated with the outer membrane and are capable of reducing cytochrome c or ferricyanide. They differ from other plant mitochondria in the apparent lack of the NADH dehydrogenase located on the outer surface of the inner membrane. |
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| 202453 | Meijer EM, Wever R, Stouthamer AH: The role of iron- center 2 in electron transport and energy conservation in the - segment of the respiratory chain in Paracoccus denitrificans. Eur J Biochem. 1977 Dec 1;81(2):267-75. Sulphate-limited growth of Paracoccus denitrificans results in the loss of an electron paramagnetic resonance signal (gz approximately 2.05, gy approximately gx approximately 1.92) which has properties similar to those of iron- center 2 of the NADH dehydrogenase of mitochondrial origin. In addition respiration in membrane particles from sulphate-limited cells loses its sensitivity to rotenone. 3. |
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| 11102582 | Thiffault C, Langston JW, Di Monte DA: Increased striatal turnover following acute administration of rotenone to mice. Brain Res. 2000 Dec 8;885(2):283-8. Because of the potential role of mitochondrial dysfunction in nigrostriatal degeneration in Parkinson's disease, the effects of rotenone (an inhibitor of mitochondrial NADH dehydrogenase and a naturally occurring toxicant) on the levels of striatal (DA) and DA metabolites were evaluated after acute and subchronic administration to mice. |
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| 3011316 | Fischer JC, Ruitenbeek W, Trijbels JM, Veerkamp JH, Stadhouders AM, Sengers RC, Janssen AJ: Estimation of oxidation in human skeletal muscle mitochondria. . Clin Chim Acta. 1986 Mar 28;155(3):263-73. The procedures allow determination of rotenone-sensitive O2 oxidoreductase and oxidoreductase activity not only in isolated mitochondria but also in post-nuclear supernatants. The use of ferricyanide as electron acceptor for estimation of NADH dehydrogenase activity is inadequate when only applied on a disrupted mitochondrial preparation. |
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| 11928630 | Hovorukha TM, Nazarenko AI, Zhalilo LI, Fil' HB, Baban VM, Seredenko MM: [Disturbances in biliary secretion during tissue hypoxia and attempts at their corrections]. Fiziol Zh. 2002;48(1):35-40. In acute experiments on rats in vivo the stimulating effects of hydrophilic cholic acids (CA and UDCA) on the bilification and their inhibiting by rotenone have been shown. |
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| 168827 | Schwartz AC, Sporkenbach J: The electron transport system of the anaerobic Propionibacterium shermanii: cytochrome and inhibitor studies. Arch Microbiol. 1975 Mar 10;102(3):261-73. The inhibitory effects of amytal and rotenone on oxidation, but not on the oxidation of the other substrates, indicated the presence of the NADH dehydrogenase complex, or "site I region", in the electron transport system of P. shermanii. 4. |
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| 1777518 | Kolesova GM, Karnaukhova LV, Iaguzhinskii LS: [Interaction of and duroquinone with Q-cycle during DT-diaphorase function]. Biokhimiia. 1991 Oct;56(10):1779-86. At 90 microM K3 50% of is reduced by DT-diaphorase and 50% by the respiratory chain NADH dehydrogenase complex enzymes; about 30% of K3H2 is oxidized via the Q-cycle, about 20%--by the terminal part of the respiratory chain and about 50%--by O2 without cytochrome oxidase. |
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| 12385818 | Alam M, Schmidt WJ: Rotenone destroys dopaminergic neurons and induces parkinsonian symptoms in rats. Behav Brain Res. 2002 Oct 17;136(1):317-24. Rotenone (an inhibitor of mitochondrial NADH dehydrogenase, a naturally occurring toxin and a commonly used pesticide) appears to reproduce the neurochemical, neuropathological and behavioural feature of Parkinson's disease (PD) in the rat. |
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| 8595975 | Soole KL, Menz RI: Functional molecular aspects of the NADH dehydrogenases of plant mitochondria. J Bioenerg Biomembr. 1995 Aug;27(4):397-406. These are the phosphorylating NADH dehydrogenase, otherwise known as Complex I, and at least four other nonphosphorylating NAD (P) H dehydrogenases. It has at least 32 polypeptides associated with it, contains FMN as its prosthetic group, and the purified enzyme is sensitive to inhibition by rotenone. |
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| 9070626 | Sriram K, Pai KS, Boyd MR, Ravindranath V: Evidence for generation of oxidative stress in brain by MPTP: in vitro and in vivo studies in mice. Brain Res. 1997 Feb 21;749(1):44-52. Pretreatment of mouse brain slices, in vitro, with GSH or GSH isopropyl ester attenuated MPTP toxicity as assessed by the tissue activity of the mitochondrial enzyme, NADH-dehydrogenase -DH), and by leakage of the cytosolic enzyme, lactate dehydrogenase (LDH), from the slice into the medium. In the striatum significant inhibition of rotenone-sensitive oxido-reductase (Complex 1) was observed transiently 1 h after MPTP administration. |
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| 10515594 | Bailey SM, Pietsch EC, Cunningham CC: stimulates the production of reactive oxygen species at mitochondrial complexes I and III. Free Radic Biol Med. 1999 Oct;27(7-8):891-900. Rotenone, a mitochondrial complex I inhibitor that allows electron flow through the (FMN), but prevents electron flow to complex III, significantly increased reactive species production in untreated cells, but decreased reactive species production in antimycin plus -treated cells. |
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| 7611477 | Pagano PJ, Ito Y, Tornheim K, Gallop PM, Tauber AI, Cohen RA: An oxidase -generating system in the rabbit aorta. . Am J Physiol. 1995 Jun;268(6 Pt 2):H2274-80. The inhibitors of xanthine oxidase, (300 microM), and of mitochondrial NADH dehydrogenase, rotenone (50 microM), had no significant effect on levels. |
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| 2645827 | MacDonald MJ, Fahien LA, Mertz RJ, Rana RS: Effect of esters of and other cycle intermediates on insulin release and formation by pancreatic islets. Arch Biochem Biophys. 1989 Mar;269(2):400-6. Since is believed to enter metabolism at site II of the mitochondrial respiratory chain, it is interesting that rotenone, an inhibitor of NADH dehydrogenase and site I of the respiratory chain, was a potent inhibitor of monomethyl -induced insulin released. Since is believed to enter metabolism at site II of the mitochondrial respiratory chain, it is interesting that rotenone, an inhibitor of NADH dehydrogenase and site I of the respiratory chain, was a potent inhibitor of monomethyl -induced insulin released. |
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| 12062413 | Svensson AS, Johansson FI, Moller IM, Rasmusson AG: Cold stress decreases the capacity for respiratory oxidation in potato leaves. FEBS Lett. 2002 Apr 24;517(1-3):79-82. The nda1 and ndb1 genes, homologues to genes encoding the non--pumping respiratory chain NADH dehydrogenases of Escherichia coli and yeast, were compared to genes encoding catalytic subunits of the -pumping NADH dehydrogenase (complex I). This decrease is accompanied by specific decreases of immunodetected NDA protein and internal rotenone-insensitive oxidation in mitochondria isolated from cold-treated plants. |
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| 8886280 | Shankar CS, Ahamad PY, Ramakrishnan MS, Umesh-Kumar S: Mitochondrial NADH dehydrogenase activity and ability to tolerate determine faster production in Saccharomyces cerevisiae. Biochem Mol Biol Int. 1996 Sep;40(1):145-50. In rapidly fermenting yeast, the rotenone insensitive mitochondrial NADH dehydrogenase was not completely repressed by high |
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| 17241123 | Sherer TB, Richardson JR, Testa CM, Seo BB, Panov AV, Yagi T, Matsuno-Yagi A, Miller GW, Greenamyre JT: Mechanism of toxicity of pesticides acting at complex I: relevance to environmental etiologies of Parkinson's disease. J Neurochem. 2007 Mar;100(6):1469-79. Epub 2007 Jan 4. The pesticide rotenone (ROT) inhibits complex I and reproduces features of PD in animal models, suggesting that environmental agents that inhibit complex I may contribute to PD. Neuroblastoma cells stably expressing the ROT-insensitive NADH dehydrogenase of Saccharomyces cerevisiae (NDI1) were resistant to these pesticides, demonstrating the requirement of complex I inhibition for toxicity. |
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| 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. The -translocating NADH dehydrogenase (NDH1) of E. coli is more sensitive to OP than is NDH1 of Paracoccus. |
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| 20207656 | Abdulwahid Arif I, Ahmad Khan H: Environmental toxins and Parkinson's disease: putative roles of impaired electron transport chain and oxidative stress. Toxicol Ind Health. 2010 Mar;26(2):121-8. Exposure of environmental chemicals such as 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and rotenone in mouse produces the symptoms akin to PD and therefore these neurotoxins are commonly used in experimental studies on PD. The neurotoxicity of these chemicals is accompanied by the blockade of electron flow from NADH dehydrogenase to |
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| 16663145 | Laties GG: Membrane-Associated NAD-Dependent Isocitrate Dehydrogenase in Potato Mitochondria. Plant Physiol. 1983 Aug;72(4):953-958. Whereas in intact mitochondria the activity of the membrane-bound enzyme is insensitive to rotenone, and to butylmalonate, an inhibitor of organic acid transport, oxidation by the soluble matrix enzyme is inhibited by both. |
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| 37082 | Meijer EM, van der Zwaan JW, Wever R, Stouthamer AH: Anaerobic respiration and energy conservation in Paracoccus denitrificans. Eur J Biochem. 1979 May 2;96(1):69-76. Furthermore respiratory chain-linked electron transport and its inhibition by rotenone are not influenced. |
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| 14732287 | Herrera B, Murillo MM, Alvarez-Barrientos A, Beltran J, Fernandez M, Fabregat I: Source of early reactive species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes. Free Radic Biol Med. 2004 Jan 1;36(1):16-26. Rotenone, an inhibitor of the NADH dehydrogenase in mitochondrial complex I, attenuated, but did not completely inhibit, ROS-production, caspase activation, and cell death mediated by TGF-beta. |
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| 9526046 | Corneille S, Cournac L, Guedeney G, Havaux M, Peltier G: Reduction of the plastoquinone pool by exogenous and in higher plant chloroplasts. Biochim Biophys Acta. 1998 Jan 27;1363(1):59-69. The NAD (P) H-PQ oxidoreductase reaction was inhibited by diphenylene iodonium, N-ethylmaleimide and dicoumarol, but insensitive to rotenone, antimycin A and piericidin A. The nature of this enzyme is discussed in relation to the existence of a thylakoidal NADH dehydrogenase complex encoded by plastidial ndh genes. |
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| 3378042 | Yagi T, Hon-nami K, Ohnishi T: Purification and characterization of two types of -quinone reductase from Thermus thermophilus HB-8. Biochemistry. 1988 Mar 22;27(6):2008-13. The occurrence of two distinct types of NADH dehydrogenase as a common feature in the membranes of various aerobic bacteria is discussed. The - reductase activity of the isolated NADH dehydrogenase 1 was about 14 times higher than that of the dodecyl beta-maltoside extract and partially rotenone sensitive. |
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| 9466828 | Kwong LK, Sohal RS: Substrate and site specificity of peroxide generation in mouse mitochondria. Arch Biochem Biophys. 1998 Feb 1;350(1):118-26. Respiratory inhibitors, antimycin and rotenone, were added singly and sequentially to each substrate-supported H2O2 generation reaction mixture to determine the mitochondrial site (s) of generation and the optimal condition (s) for maximal rates of generation. The contribution from each of the three sites NADH dehydrogenase, and dehydrogenase) of mitochondrial H2O2 generation to the total was both substrate and organ dependent. |
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| 11696188 | Svensson AS, Rasmusson AG: Light-dependent gene expression for proteins in the respiratory chain of potato leaves. Plant J. 2001 Oct;28(1):73-82. The recently characterized nda1 and ndb1 genes, homologues to genes encoding the non- pumping respiratory chain NADH-dehydrogenases of Escherichia coli and yeast, were compared to genes encoding catalytic subunits of the -pumping NADH dehydrogenase (complex I). As leaves develop from young to mature, the nda1 transcript level increases, accompanied by an elevation in immunodetected NDA protein and internal rotenone-insensitive oxidation. |
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| 8392019 | Sohal RS: Aging, cytochrome oxidase activity, and peroxide release by mitochondria. Free Radic Biol Med. 1993 Jun;14(6):583-8. Results are interpreted to suggest that partial inhibition of cytochrome c oxidase activity can lead to the stimulation of mitochondrial H2O2 production in the housefly at site (s) other than NADH dehydrogenase and /cytochrome b region; a possible source may be glycerophosphate dehydrogenase. H2O2 release by mitochondria, inhibited with rotenone and antimycin A, was greatly increased upon supplementation with however, the further addition of KCN or myxothiazol, to such preparations, caused a depression of H2O2 generation. |
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| 2321971 | Bolter CJ, Chefurka W: Extramitochondrial release of peroxide from insect and mouse liver mitochondria using the respiratory inhibitors phosphine, myxothiazol, and antimycin and spectral analysis of inhibited cytochromes. Arch Biochem Biophys. 1990 Apr;278(1):65-72. Other respiratory inhibitors, antimycin, myxothiazol, and rotenone were used with insect mitochondria. |
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| 9824492 | Carrasco-Marin E, Paz-Miguel JE, Lopez-Mato P, Alvarez-Dominguez C, Leyva-Cobian F: Oxidation of defined antigens allows protein unfolding and increases both proteolytic processing and exposes peptide epitopes which are recognized by specific T cells. Immunology. 1998 Nov;95(3):314-21. However, neither rotenone and antimycins (inhibitors of O-2 production at the NADH dehydrogenase and -cytochrome b regions, respectively) nor aminoguanidine (an inducible synthase inhibitor) impaired antigen presentation, thus indirectly discarding the participation of mitochondrial oxidation and reactive intermediates (RNI) in antigen processing. |
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| 3486869 | Ramsay RR, Singer TP: Energy-dependent uptake of N-methyl-4-phenylpyridinium, the metabolite of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, by mitochondria. J Biol Chem. 1986 Jun 15;261(17):7585-7. The latter is widely believed to be the compound responsible for neuronal destruction and the NADH dehydrogenase of the inner membrane has been postulated to be its target. |
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| 10347173 | Barrientos A, Moraes CT: Titrating the effects of mitochondrial complex I impairment in the cell physiology. J Biol Chem. 1999 Jun 4;274(23):16188-97. NADH dehydrogenase or complex I (CI) is affected in most of the mitochondrial diseases and in some neurodegenerative disorders. We used a genetic model (40% CI-inhibited human-ape xenomitochondrial cybrids) and a drug-induced model (0-100% CI-inhibited cells using different concentrations of rotenone). |
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| 4323963 | Wong DT, Horng JS, Gordee RS: Respiratory chain of a pathogenic fungus, Microsporum gypseum: effect of the antifungal agent pyrrolnitrin. J Bacteriol. 1971 Apr;106(1):168-73. In mitochondrial preparations, pyrrolnitrin strongly inhibited respiration and the rotenone-sensitive -cytochrome c reductase. We, therefore, concluded that the primary site of action of this antifungal antibiotic is to block electron transfer between the flavoprotein of the NADH-dehydrogenase and cytochrome b segment of the respiratory chain of M. gypseum. |
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| 8806050 | Sablin SO, Krueger MJ, Yankovskaya VL, Tkachenko SE, Razdolsky AN, Bachurin SO, Ramsay RR, Singer TP: Inhibition of oxidation by 1-methyl-4-phenylpyridinium analogs as the basis for the prediction of the inhibitory potency of novel compounds. J Biochem Toxicol. 1996;11(1):33-43. Inhibition of NADH dehydrogenase (Complex I) of the mitochondrial respiratory chain by 1-methyl-4-phenylpyridinium (MPP+) and its analogs results in dopaminergic cell death. The IC50 values for these compounds and previously published figures for MPP+ analogs were then used to select a computer model based on structural parameters to predict the inhibitory potency of other compounds that react at the "rotenone site" in Complex I. |
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| 3005279 | Doroshow JH, Davies KJ: Redox cycling of anthracyclines by cardiac mitochondria. J Biol Chem. 1986 Mar 5;261(7):3068-74. In the presence of rotenone, initial rates of consumption and formation were identical under comparable experimental conditions. These experiments suggest that injury to cardiac mitochondria which is produced by anthracycline antibiotics may result from the generation of the during anthracycline metabolism by NADH dehydrogenase. |
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| 3138118 | de Vries S, Grivell LA: Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur J Biochem. 1988 Sep 15;176(2):377-84. The purified NADH dehydrogenase consists of a single subunit with molecular mass of 53 kDa as indicated by SDS/polyacrylamide gel electrophoresis. |
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| 8106350 | Gluck MR, Krueger MJ, Ramsay RR, Sablin SO, Singer TP, Nicklas WJ: Characterization of the inhibitory mechanism of 1-methyl-4-phenylpyridinium and 4-phenylpyridine analogs in inner membrane preparations. J Biol Chem. 1994 Feb 4;269(5):3167-74. We have investigated the mechanism of the inhibition of membrane-bound NADH dehydrogenase by 1-methyl-4-phenylpyridinium (MPP+) and a series of its 4'-alkyl-substituted analogs of increasing hydrophobicity, as well as their neutral, desmethyl congeners. These data support the hypothesis that MPP+ analogs, like rotenone, are bound at two sites on the enzyme and occupancy of both is required for complete inhibition. |
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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. The steady-state kinetics of the NADH dehydrogenase activities of the mitochondrial NADH-ubiquinone oxidoreductase in the presence of one-electron acceptors, ferricyanide and hexammineruthenium (III), were studied. Both hexammineruthenium (III) and ferricyanide reduction was rotenone-insensitive and showed no stimulation by the uncouplers in tightly coupled submitochondrial particles. |
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| 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. ADPR competitively inhibits oxidation with Ki values (25 degrees C, pH 8.0) of 26 microM, 30 microM, and 180 microM for SMP, purified Complex I and three-subunit NADH dehydrogenase (FP), respectively. Ki for inhibition of the rotenone-sensitive oxidase in SMP by ADPR does not depend on delta mu H+. |
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| 4296021 | Kaniuga Z, Gardas A, Jakubiak M: Studies on the respiratory chain-linked dehydrogenase. Biochim Biophys Acta. 1968 Feb 12;153(2):317-28. Effect of diethyl ether on particulate NADH dehydrogenase. |
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| 7628058 | Poderoso JJ, Fernandez S, Carreras MC, Tchercanski D, Acevedo C, Rubio M, Peralta J, Boveris A: Liver uptake dependence and mitochondrial function in septic rats. Circ Shock. 1994 Dec;44(4):175-82. In submitochondrial, only NADH-dehydrogenase activity was 100% higher in septic samples. |
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| 3094534 | Suzuki H, Wakai M, Ozawa T: Selective inhibition of mitochondrial -ubiquinone reductase (Complex I) by an alkyl polyoxyethylene ether. Biochem Int. 1986 Aug;13(2):351-7. The detergent inhibited rotenone-sensitive -ubiquinone reductase activity, but not -ferricyanide reductase activity, of isolated Complex I. These results show that the binding site of the detergent responsible for the inhibition lies between the NADH dehydrogenase of flavoprotein and in Complex I and that the binding of the detergent to the site requires phospholipids. |
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| 12678433 | Fernandes AS, Pereira MM, Teixeira M: Purification and characterization of the complex I from the respiratory chain of Rhodothermus marinus. J Bioenerg Biomembr. 2002 Dec;34(6):413-21. The rotenone sensitive NADH:menaquinone oxidoreductase (NDH-I or complex I) from the thermohalophilic bacterium Rhodothermus marinus has been purified and characterized. The optimum conditions for NADH dehydrogenase activity are 50 degrees C and pH 8.1, and the enzyme presents a KM of 9 microM for |
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| 18414996 | Benit P, Slama A, Rustin P: Decylubiquinol impedes mitochondrial respiratory chain complex I activity. Mol Cell Biochem. 2008 Jul;314(1-2):45-50. Epub 2008 Apr 15. Use of these conditions is however restricted to tissues/cells with limited contaminating NADH dehydrogenase activities that are prone to react with redox active compounds. |
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| 2574998 | Levin GS, Tremasova GIa, Kostova SV, Dregeris IaIa: [The mechanism of action of a synthetic derivative of 1,4-naphthoquinone on the respiratory chain of liver and heart mitochondria]. Biokhimiia. 1989 Oct;54(10):1630-7. AK-135 fully restores the rate of (but not oxidation by liver and heart mitochondria catalyzed by rotenone, antimycin A and The experimental results suggest that in the liver and heart AK-135 accepts electrons from NADH-dehydrogenase oxidizing endogenous |
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| 10220277 | Konishi K, Tanaka T: Inhibitory effects of tannins on the NADH dehydrogenase activity of bovine heart mitochondrial complex I. Biol Pharm Bull. 1999 Mar;22(3):240-3. Although many specific inhibitors of NDH-1 (e.g. rotenone and piericidin A) have been reported, the reactive sites are at or near to, the -binding site. |
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| 7174640 | Imagawa T, Kasai S, Matsui K, Nakamura T: Methyl hydroperoxy-epoxy-octadecenoate as an autoxidation product of methyl a new inhibitor-uncoupler of mitochondrial respiration. J Biochem. 1982 Oct;92(4):1109-21. -acceptor reductase activities of submitochondrial particles were inhibited by ML-X to the same extents as by rotenone. These findings show that ML-X has dual effects on mitochondrial respiration as (1) an inhibitor of NADH dehydrogenase complex and (2) an uncoupler. |
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| 727852 | Meijer EM, Schuitenmaker MG, Boogerd FC, Wever R, Stouthamer AH: Effects induced by rotenone during aerobic growth of Paracoccus denitrificans in continuous culture. Arch Microbiol. 1978 Nov 13;119(2):119-27. Changes in energy conservation and electron transport associated with NADH dehydrogenase. |
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| 2846570 | Krishnamoorthy G, Hinkle PC: Studies on the electron transfer pathway, topography of iron- centers, and site of coupling in -Q oxidoreductase. J Biol Chem. 1988 Nov 25;263(33):17566-75. The results suggest that bound, reduced nucleotide, probably E-NAD., is the main source of O2- in NADH dehydrogenase. N-Bromosuccinimide also destroyed the signal from N-4 but without inhibiting rotenone-sensitive electron transfer to suggesting a branched pathway for electron transfer. |
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| 427130 | Kilberg MS, Christensen HN: Electron-transferring enzymes in the plasma membrane of the Ehrlich ascites tumor cell. Biochemistry. 1979 Apr 17;18(8):1525-30. The activity differed from that of the mitochondria in that it was not inhibited by rotenone or antimycin A. The plasma membrane of the Ehrlich ascites tumor cell contains an NADH dehydrogenase. |
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| 7084467 | Phillips MK, Kell DB: A novel inhibitor of NADH dehydrogenase in Paracoccus denitrificans. FEBS Lett. 1982 Apr 19;140(2):248-50. |
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| 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. In parallel there was a 50% reduction in mRNA levels for the mitochondrially encoded nd1 gene, a subunit of the NADH dehydrogenase comprising complex I of the mitochondrial respiratory chain. Rotenone, an inhibitor of complex I, mimicked this effect. |
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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. In mitochondria from all the strains analyzed, we moreover detected a 160-210 kDa fragment comprising the hydrophilic 49 kDa and 76 kDa subunits of the complex I peripheral arm and showing NADH dehydrogenase activity. |
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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. In vascular plants, fungi, and animals, at least seven complex I subunits (ND1, -2, -3, -4, -4L, -5, and -6; ND is NADH dehydrogenase) are coded by mitochondrial genes. |
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| 16581014 | Yagi T, Seo BB, Nakamaru-Ogiso E, Marella M, Barber-Singh J, Yamashita T, Matsuno-Yagi A: Possibility of transkingdom gene therapy for complex I diseases. Biochim Biophys Acta. 2006 May-Jun;1757(5-6):708-14. Epub 2006 Feb 24. Defects of complex I are involved in many human mitochondrial diseases, and therefore we have proposed to use the NDI1 gene encoding a single subunit NADH dehydrogenase of Saccharomyces cerevisiae for repair of respiratory activity. The NDI1-transduced cells were more resistant to complex I inhibitors and diminished production of reactive species induced by rotenone. |
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| 838718 | Van Dop C, Hutson SM, Lardy HA: Pyruvate metabolism in bovine epididymal spermatozoa. . J Biol Chem. 1977 Feb 25;252(4):1303-8. thus competes with, and can substitute for, the NADH dehydrogenase of the electron transport chain. Treating bovine epididymal spermatozoa with rutamycin or rotenone inhibited both respiration and motility supported by endogenous substrates. |
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| 4345350 | Barnes R, Connelly JL, Jones OT: The utilization of iron and its complexes by mammalian mitochondria. . Biochem J. 1972 Aug;128(5):1043-55. Possible sites for this reduction are the flavoproteins, and NADH dehydrogenase. The reduction was insensitive to rotenone or antimycin A. |
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| 11732343 | Nohl H, Gille L: The existence and significance of redox-cycling in lysosomes. . Protoplasma. 2001;217(1-3):9-14. Analysis of the components involved in the transfer of reducing equivalents from cytosolic to revealed the existence of a -containing NADH dehydrogenase. |
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| 8037664 | Degli Esposti M, Ghelli A, Ratta M, Cortes D, Estornell E: Natural substances (acetogenins) from the family Annonaceae are powerful inhibitors of mitochondrial NADH dehydrogenase (Complex I). Biochem J. 1994 Jul 1;301 ( Pt 1):161-7. The properties of five of such acetogenins are compared with those of rotenone and piericidin, classical potent inhibitors of Complex I. |
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| 17320357 | Park JS, Li YF, Bai Y: Yeast NDI1 improves oxidative phosphorylation capacity and increases protection against oxidative stress and cell death in cells carrying a Leber's hereditary optic neuropathy mutation. Biochim Biophys Acta. 2007 May;1772(5):533-42. Epub 2007 Jan 26. G11778A in the subunit ND4 gene of NADH dehydrogenase complex is the most common primary mutation found in Leber's hereditary optic neuropathy (LHON) patients. In transformant cell lines, LeNDI1-1 and -2, total and complex I-dependent respiration were fully restored and largely resistant to complex I inhibitor, rotenone, indicating a dominant role of NDI1 in the transfer of electrons in the host cells. |
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| 4152604 | Green AP, Hooper M, Sweetman AJ: The interaction of 2-phenylisatogen and with rat liver mitochondrial NADH dehydrogenase. Biochem Pharmacol. 1974 May 1;23(11):1569-76. |
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| 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. -uptake experiments, performed with mitochondria isolated from the mutant cells, showed that this NADH dehydrogenase catalyzes the oxidation of generated inside 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 azide, antimycin A, and 2-heptyl-4-hydroxyquinoline-N-oxide, but was relatively resistant to rotenone and amytal. |
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| 12840017 | Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL, Lesnefsky EJ: Production of reactive species by mitochondria: central role of complex III. J Biol Chem. 2003 Sep 19;278(38):36027-31. Epub 2003 Jul 2. ROS are produced from complex I by the NADH dehydrogenase located in the matrix side of the inner membrane and are dissipated in mitochondria by matrix antioxidant defense. Limitation of electron transport by the inhibitor rotenone immediately before ischemia decreases the production of ROS in cardiac myocytes and reduces damage to mitochondria. |
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| 7999034 | Pecci L, Fontana M, Montefoschi G, Cavallini D: Aminoethylcysteine ketimine decarboxylated dimer protects submitochondrial particles from lipid peroxidation at a concentration not inhibitory of electron transport. Biochem Biophys Res Commun. 1994 Nov 30;205(1):264-8. In contrast with other inhibitors of the NADH dehydrogenase of the respiratory chain, the decarboxylated dimer of aminoethylcysteine ketimine protects bovine heart submitochondrial particles (SMP) from the -Fe (+3)--induced lipid peroxidation. Furthermore the dimer is able to counteract the malondialdehyde formation stimulated by the Complex I inhibitors rotenone and N-methyl-4-phenylpyridinium (MPP+). |
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| 6667089 | McEwan AG, Ferguson SJ, Jackson JB: Electron flow to dimethylsulphoxide or generates a membrane potential in Rhodopseudomonas capsulata. Arch Microbiol. 1983 Dec;136(4):300-5. The magnitude of the dimethylsulphoxide- or -dependent membrane potential was reduced either by a protonophore uncoupler of oxidative phosphorylation or synergistically by a combination of a protonophore plus rotenone, an inhibitor of electron flow from NADH dehydrogenase. The magnitude of the dimethylsulphoxide- or -dependent membrane potential was reduced either by a protonophore uncoupler of oxidative phosphorylation or synergistically by a combination of a protonophore plus rotenone, an inhibitor of electron flow from NADH dehydrogenase. |
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