| Name | NADH dehydrogenases (protein family or complex) |
|---|---|
| Synonyms | NADH dehydrogenase; NADH dehydrogenases |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 7941733 | Buschges R, Bahrenberg G, Zimmermann M, Wolf K: oxidoreductase in obligate aerobic yeasts. Yeast. 1994 Apr;10(4):475-9. These species show in all growth phases and under standard cultivation conditions, NADH dehydrogenases of approximately 700 kDa, which are sensitive to rotenone, a specific inhibitor of this complex. |
32(0,1,1,2) | Details |
| 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. The oxidation of matrix and cytosolic by isolated beetroot and wheat leaf mitochondria was investigated to determine whether the rotenone-insensitive NADH dehydrogenases of plant mitochondria were the products of nuclear or mitochondrial genes. |
32(0,1,1,2) | Details |
| 11245784 | Joseph-Horne T, Hollomon DW, Wood PM: Fungal respiration: a fusion of standard and alternative components. Biochim Biophys Acta. 2001 Apr 2;1504(2-3):179-95. These consist of alternative NADH dehydrogenases, which catalyse rotenone insensitive oxidation of matrix or enable cytoplasmic to be used directly. |
32(0,1,1,2) | Details |
| 10571867 | Rasmusson AG, Svensson AS, Knoop V, Grohmann L, Brennicke A: Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: two enzymes are present in potato mitochondria. Plant J. 1999 Oct;20(1):79-87. |
18(0,0,3,3) | Details |
| 198640 | Sokolov GV, Eremina SS, Lozinov AB: [Respiratory chain of Candida mycoderma] . Mikrobiologiia. 1977 Jul-Aug;46(4):597-604. Two flavoprotein NADH-dehydrogenases are present in the cells of C. mycoderma: one is sensitive to rotenone, the other is resistant to it. |
7(0,0,1,2) | Details |
| 14731260 | Michalecka AM, Agius SC, Moller IM, Rasmusson AG: Identification of a mitochondrial external dehydrogenase by overexpression in transgenic Nicotiana sylvestris. Plant J. 2004 Feb;37(3):415-25. Activities of external and internal rotenone-insensitive NADH dehydrogenases were unchanged in the transgenic lines. |
6(0,0,1,1) | Details |
| 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. |
6(0,0,1,1) | Details |
| 2249975 | Dreyer JL: Plasma membrane dehydrogenases in rat brain synaptic membranes. J Bioenerg Biomembr. 1990 Oct;22(5):619-33. The molecular characterization of rat synaptic NADH-dehydrogenases was further performed on solubilized enzymes using a recently developed nondissociating polyacrylamide gel electrophoresis technique. Both enzyme activities were insensitive toward rotenone. |
3(0,0,0,3) | 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. |
3(0,0,0,3) | 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. |
2(0,0,0,2) | Details |
| 12758076 | Marques I, Duarte M, Videira A: The 9.8 kDa subunit of complex I, related to bacterial Na (+)-translocating NADH dehydrogenases, is required for enzyme assembly and function in Neurospora crassa. J Mol Biol. 2003 May 30;329(2):283-90. Respiration of mutant mitochondria on matrix is rotenone-insensitive, confirming that the 9.8 kDa protein is required for the assembly and activity of complex I. |
2(0,0,0,2) | 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. It contains a covalently attached flavin, which was identified as being FMN by 31P-NMR spectroscopy, a novelty among type-II NADH dehydrogenases. |
1(0,0,0,1) | Details |
| 18251845 | Juszczuk IM, Flexas J, Szal B, Dabrowska Z, Ribas-Carbo M, Rychter AM: Effect of mitochondrial genome rearrangement on respiratory activity, photosynthesis, photorespiration and energy status of MSC16 cucumber (Cucumis sativus) mutant. Physiol Plant. 2007 Dec;131(4):527-41. Decreased respiratory capacity of complex I in MSC16 mitochondria was indicated by lower respiration rates of intact mitochondria with and by rotenone-inhibited or oxidation in the presence of alamethicin. Concerning the redox state, complex I impairment could be compensated to some extent by increased external NADH dehydrogenases (ND (ex) and alternative oxidase (AOX) capacity, the latter presenting differential expression in the light and in the dark. |
1(0,0,0,1) | Details |
| 1497658 | Sivan VM, Raj RK: dependent dehydrogenation in mitochondria-like particles from Setaria digitata, a filarial parasite. Biochem Biophys Res Commun. 1992 Jul 31;186(2):698-705. In the cattle filarial parasite, Setaria digitata, the mitochondria-like particles have been shown to possess site I associated oxidative phosphorylation and rotenone sensitive and insensitive pathways for the dehydrogenation of depleted mitochondria-like particles show a loss of activity of these NADH dehydrogenases and also a complete loss of reductase activity. |
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). The absence of such "alternative" NADH dehydrogenases in the human host defines these enzymes as potential drug targets. |
1(0,0,0,1) | Details |
| 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 relation of this enzyme with respect to various other NADH dehydrogenases from yeast and plant mitochondria is discussed. |
1(0,0,0,1) | Details |
| 20185797 | Ago T, Kuroda J, Pain J, Fu C, Li H, Sadoshima J: Upregulation of Nox4 by Hypertrophic Stimuli Promotes Apoptosis and Mitochondrial Dysfunction in Cardiac Myocytes. Circ Res. 2010 Feb 25. Nox4 is primarily localized in mitochondria and upregulation of Nox4 enhanced both rotenone- and diphenyleneiodonium-sensitive O2 (.-) production in mitochondria. residues in mitochondrial proteins, including aconitase and NADH dehydrogenases, were oxidized and their activities decreased in Tg-Nox4. |
1(0,0,0,1) | 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. Rather, they resulted from thermodynamic properties of these two oxidases and the kinetics of the two NADH dehydrogenases found in plant mitochondria. At low concentrations the rotenone-sensitive NADH dehydrogenase was active and could accept electrons from both oxidases. |
1(0,0,0,1) | Details |
| 6819864 | Palmer JM, Schwitzguebel JP, Moller IM: Regulation of oxidation in plant mitochondria. Biochem J. 1982 Dec 15;208(3):703-11. Exogenous NAD+ stimulated the rotenone-resistant oxidation of all the NAD+-linked tricarboxylic acid-cycle substrates in mitochondria from Jerusalem artichoke (Helianthus tuberosus L.) tubers. Thus it is proposed that the concentration of regulates the activity of the two internal NADH dehydrogenases. |
1(0,0,0,1) | Details |
| 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. An open reading frame homologous with genes of non--pumping NADH dehydrogenases was identified in the genome of Neurospora crassa. 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. |
1(0,0,0,1) | Details |
| 8595975 | Soole KL, Menz RI: Functional molecular aspects of the NADH dehydrogenases of plant mitochondria. J Bioenerg Biomembr. 1995 Aug;27(4):397-406. 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. |
1(0,0,0,1) | Details |
| 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 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. |
1(0,0,0,1) | Details |
| 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. These results suggest that the tannins are potent inhibitors of NADH dehydrogenases, and that the inhibitory mechanisms are novel. 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. |
1(0,0,0,1) | Details |
| 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. |
1(0,0,0,1) | Details |
| 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. Both NADH dehydrogenases contain in the central part of the protein a sequence predicted to fold into a beta alpha beta structure involved in the binding of or FAD (H2). |
1(0,0,0,1) | 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. Soluble -cytochrome c-oxidoreductase (MAHLER) and rotenone-insensitive ubiquinone reductase are also inhibited by dexon. |
1(0,0,0,1) | Details |
| 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. |
1(0,0,0,1) | 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. The non-ionic detergent lauryl N-oxide (LDAO) has been used to extract the NADH dehydrogenases of Arum maculatum mitochondria. |
1(0,0,0,1) | Details |
| 1521539 | Menz RI, Griffith M, Day DA, Wiskich JT: Matrix NADH dehydrogenases of plant mitochondria and sites of reduction by complex I. Eur J Biochem. 1992 Sep 1;208(2):481-5. --dinucleotide (reduced form)-oxidase activity was more strongly inhibited by rotenone than the -oxidase activity but both of the rotenone-inhibited activities could be stimulated by adding |
1(0,0,0,1) | Details |
| 9096412 | Gutierres S, Sabar M, Lelandais C, Chetrit P, Diolez P, Degand H, Boutry M, Vedel F, de Kouchkovsky Y, De Paepe R: Lack of mitochondrial and nuclear-encoded subunits of complex I and alteration of the respiratory chain in Nicotiana sylvestris mitochondrial deletion mutants. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3436-41. These results suggest respiratory compensation mechanisms involving additional NADH dehydrogenases to complex I. The remaining activity was much less sensitive to rotenone, indicating the breakdown of Complex I activity. |
1(0,0,0,1) | Details |
| 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. Two different high molecular weight NADH dehydrogenases were characterized by native PAGE and detected by direct in-gel activity staining. Spectrophotometric measurement of the NADH:ubiquinone 10 and NADH:ferricyanide dehydrogenase activities revealed their different sensitivities to rotenone, piericidin, and diphenyl iodonium. |
1(0,0,0,1) | Details |
| 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 activities of both NADH dehydrogenases were stable at temperatures of greater than or equal to 80 degrees C. 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. |
1(0,0,0,1) | Details |
| 14641052 | Popov VN: Possible role of free oxidation processes in the regulation of reactive species production in plant mitochondria. Biochem Soc Trans. 2003 Dec;31(Pt 6):1316-7. The non-coupled substrate oxidation mediated by components of the electron transport chain that are not coupled to energy accumulation (such as plant alternative oxidase and rotenone-insensitive NADH dehydrogenases) and uncoupled respiration are peculiar features of plant mitochondria. |
0(0,0,0,0) | 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. |
0(0,0,0,0) | Details |