| Name | electron transfer flavoprotein ubiquinone oxidoreductase |
|---|---|
| Synonyms | ETF dehydrogenase; MADD; ETF QO; ETF ubiquinone oxidoreductase; ETFDH; ETFQO; Electron transfer flavoprotein; Electron transfer flavoprotein dehydrogenase… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 3620453 | Frerman FE: Reaction of electron-transfer flavoprotein ubiquinone oxidoreductase with the mitochondrial respiratory chain. Biochim Biophys Acta. 1987 Sep 10;893(2):161-9. Submitochondrial particles catalyze the reduction of electron-transfer flavoprotein (ETF) by and under anaerobic conditions in reactions that are totally inhibited by rotenone and thenoyl trifluoroacetone, respectively. |
32(0,1,1,2) | Details |
| 8376393 | Ma YC, Funk M, Dunham WR, Komuniecki R: Purification and characterization of electron-transfer flavoprotein: rhodoquinone oxidoreductase from anaerobic mitochondria of the adult parasitic nematode, Ascaris suum. J Biol Chem. 1993 Sep 25;268(27):20360-5. Incubations of A. suum submitochondrial particles with purified A. suum electron-transfer flavoprotein and 2-methyl branched-chain enoyl- reductase resulted in significant formation, which was inhibited by both rotenone and antisera to the purified ETF-RO. |
32(0,1,1,2) | Details |
| 6704106 | Komuniecki R, Fekete S, Thissen J: 2-Methylbutyryl CoA dehydrogenase from mitochondria of Ascaris suum and its relationship to -dependent reduction. Biochem Biophys Res Commun. 1984 Feb 14;118(3):783-8. In fact, incubations of A. suum mitochondrial membranes with electron-transfer flavoprotein, 2-methylbutyryl CoA dehydrogenase, and resulted in a substantial, rotenone-sensitive, 2-methylbutyrate synthesis. |
32(0,1,1,2) | Details |
| 3988734 | Komuniecki R, Fekete S, Thissen-Parra J: Purification and characterization of the 2-methyl branched-chain Acyl-CoA dehydrogenase, an enzyme involved in -dependent enoyl- reduction in anaerobic mitochondria of the nematode, Ascaris suum. J Biol Chem. 1985 Apr 25;260(8):4770-7. Incubations of A. suum submitochondrial particles, purified A. suum electron-transfer flavoprotein, and the 2-methyl branched-chain acyl-CoA dehydrogenase resulted in the rotenone-sensitive, dehydrogenase-dependent formation of |
6(0,0,1,1) | Details |
| 19366681 | Hoffman DL, Brookes PS: sensitivity of mitochondrial reactive species generation depends on metabolic conditions. J Biol Chem. 2009 Jun 12;284(24):16236-45. Epub 2009 Apr 14. From such data, the apparent Km for O2 of putative ROS-generating sites within mitochondria was estimated as follows: 0.2, 0.9, 2.0, and 5.0 microM O2 for the complex I flavin site, complex I electron backflow, complex III QO site, and electron transfer flavoprotein quinone oxidoreductase of beta-oxidation, respectively. |
2(0,0,0,2) | Details |
| 3337800 | Kunz WS: Evaluation of electron-transfer flavoprotein and alpha- dehydrogenase redox states by two-channel fluorimetry and its application to the investigation of beta-oxidation. Biochim Biophys Acta. 1988 Jan 20;932(1):8-16. It was found that in the presence of rotenone, and a redox buffer for the mitochondrial NAD-system, the beta-oxidation flux was sensitive to variations in redox state of respiratory chain electron carriers at low states of NAD reduction. |
2(0,0,0,2) | Details |
| 1668635 | Kunz WS: Application of the theory of steady-state flux control to mitochondrial beta-oxidation. Biomed Biochim Acta. 1991;50(12):1143-57. The theory of steady-state flux control was applied to characterize the regulation of beta-oxidation flux in uncoupled rat liver mitochondria oxidizing in the presence of rotenone, and the / redox buffer. The flux control coefficients of carnitine palmitoyltransferase II, ETF:CoQ oxidoreductase and dehydrogenase were determined from elasticity coefficients obtained by measuring the flux dependencies of acyl- and acetyl-CoA+CoASH concentrations, the electron transfer flavoprotein redox state, the redox state and the NAD redox state. |
1(0,0,0,1) | Details |
| 12237311 | St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD: Topology of production from different sites in the mitochondrial electron transport chain. J Biol Chem. 2002 Nov 22;277(47):44784-90. Epub 2002 Sep 16. However, when complex I was fully reduced using rotenone, rat mitochondria released significantly more peroxide than pigeon mitochondria. Complex I (and perhaps the fatty acid oxidation electron transfer flavoprotein and its oxidoreductase) released on the matrix side of the inner membrane, whereas center o of complex III released on the cytoplasmic side. |
1(0,0,0,1) | Details |