| Name | NADH coenzyme Q reductase |
|---|---|
| Synonyms | CI 15 kDa; NADH coenzyme Q reductase; Complex I 15 kDa; NADH dehydrogenase (ubiquinone) Fe S protein 5 (15kD) (NADH coenzyme Q reductase); NADH dehydrogenase [ubiquinone] iron sulfur protein 5; NADH ubiquinone oxidoreductase 15 kDa subunit; NADH ubiquinone oxidoreductase Fe S protein 5; NDUFS 5… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 8603732 | Merlo Pich M, Bovina C, Formiggini G, Cometti GG, Ghelli A, Parenti Castelli G, Genova ML, Marchetti M, Semeraro S, Lenaz G: Inhibitor sensitivity of respiratory complex I in human platelets: a possible biomarker of ageing. FEBS Lett. 1996 Feb 12;380(1-2):176-8. NADH-Coenzyme Q reductase was assayed in platelet mitochondrial membranes obtained from 19 pools of two venous blood samples from female young (19-30 years) individuals and 18 pools from aged ones (66-107 years). The enzyme activities were not significantly changed in the two groups, but a decrease of sensitivity to the specific inhibitor, rotenone, occurred in a substantial number of aged individuals. |
1(0,0,0,1) | Details |
| 444478 | Lichtor T, Tung B, Getz GS: Cytoplasmically inherited respiratory deficiency of a mouse fibroblast line which is resistant to rutamycin. Biochemistry. 1979 Jun 12;18(12):2582-90. These cells produce large amounts of lactic acid, and consumption data indicate that the first complex of the electron transport chain, NADH-coenzyme Q reductase, is defective. Levels of rotenone-sensitive -cytochrome c reductase and decarboxylase of the pyruvate dehydrogenase complex are markedly depressed in the mutant cells. |
1(0,0,0,1) | Details |
| 1567448 | Unnikrishnan LS, Raj RK: reductase system of filarial parasite Setaria digitata. Biochem Biophys Res Commun. 1992 Apr 15;184(1):448-53. This activity is sensitive to rotenone, antimycin A and o- diphenyl. The reductase system consisting of NADH-coenzyme Q reductase, cytochrome b like component (s) and succinate dehydrogenase/ reductase is thus very important and hence specific inhibitors of the system may prove useful in the effective control of filariasis. |
1(0,0,0,1) | Details |
| 8892026 | Pitkanen S, Feigenbaum A, Laframboise R, Robinson BH: NADH-coenzyme Q reductase (complex I) deficiency: heterogeneity in phenotype and biochemical findings. J Inherit Metab Dis. 1996;19(5):675-86. Each patient also had decreased rotenone-sensitive -cytochrome c reductase (complexes I and III) with normal cytochrome c reductase (complexes II and III) and cytochrome oxidase (complex IV) activity in cultured skin fibroblasts, indicating a deficient NADH-coenzyme Q reductase (complex I) activity. |
82(1,1,1,2) | Details |
| 3106581 | Nishizawa M, Tanaka K, Shinozawa K, Kuwabara T, Atsumi T, Miyatake T, Ohama E: A mitochondrial encephalomyopathy with cardiomyopathy. J Neurol Sci. 1987 Apr;78(2):189-201. The rotenone-sensitive NADH-coenzyme Q reductase activity was markedly decreased in heart, skeletal muscle and liver mitochondria. |
6(0,0,1,1) | Details |
| 8986635 | Pitkanen S, Raha S, Robinson BH: Diagnosis of complex I deficiency in patients with lactic acidemia using skin fibroblast cultures. Biochem Mol Med. 1996 Dec;59(2):134-7. Values for -cytochrome c reductase (rotenone sensitive) were compared for a series of three controls and nine patients with complex I (NADH-coenzyme Q reductase deficiency). |
6(0,0,1,1) | Details |
| 9309707 | Lenaz G, Bovina C, Castelluccio C, Fato R, Formiggini G, Genova ML, Marchetti M, Pich MM, Pallotti F, Parenti Castelli G, Biagini G: Mitochondrial complex I defects in aging. Mol Cell Biochem. 1997 Sep;174(1-2):329-33. According to the 'mitochondrial theory of aging' it is expected that the activity of NADH Coenzyme Q reductase (Complex I) would be most severely affected among mitochondrial enzymes, since mitochondrial DNA encodes for 7 subunits of this enzyme. A decrease of oxidation and its rotenone sensitivity was observed in nonsynaptic mitochondria, but not in synaptic 'light' and 'heavy' mitochondria of brain cortex from aged rats. |
2(0,0,0,2) | Details |
| 386 | Ragan CI, Hinkle PC: Ion transport and respiratory control in vesicles formed from reductase and phospholipids. J Biol Chem. 1975 Nov 10;250(21):8472-6. NADH-coenzyme Q reductase from bovine heart mitochondria (complex I) was incorporated into phospholipid vesicles by the dialysis procedure. |
2(0,0,0,2) | Details |
| 947896 | DeFrancesco L, Scheffler IE, Bissell MJ: A respiration-deficient Chinese hamster cell line with a defect in NADH-coenzyme Q reductase. J Biol Chem. 1976 Aug 10;251(15):4588-95. The conclusion is based on the following observations. (a) In this and in the earlier report we determined that the relevant enzymes of the Krebs cycle are present and active. (b) consumption by isolated mitochondria is normal when driven by and alpha-glycerolphosphate. (c) Difference spectra between reduced and oxidized forms indicate that all cytochromes are present and functional. (d) In contrast, substrates such as alpha-ketoglutarate, and which generate do not stimulate consumption in mutant mitochondria. (e) A direct assay of the rotenone-sensitive oxidase in Lubrol-treated mitochondria from mutant cells revealed less than one-tenth of the activity when compared with wild type mitochondria. (f) The treatment of wild type cells with rotenone, a specific inhibitor of - reductase, yielded an exact phenocopy of the mutant by several criteria. |
2(0,0,0,2) | Details |
| 3100753 | Kobayashi M, Morishita H, Sugiyama N, Yokochi K, Nakano M, Wada Y, Hotta Y, Terauchi A, Nonaka I: Two cases of NADH-coenzyme Q reductase deficiency: relationship to MELAS syndrome. J Pediatr. 1987 Feb;110(2):223-7. Rotenone-sensitive cytochrome c reductase activities were decreased to 8% (patient 1) and 6% (patient 2) of control values; cytochrome c reductase and cytochrome c oxidase values were within normal limits. |
1(0,0,0,1) | Details |