| Name | NADH cytochrome b5 reductase |
|---|---|
| Synonyms | B5R; CYB5R; CYB5R3; Cytochrome b5 reductase 3; Cytochrome b5 reductase; DIA 1; DIA1; Diaphorase (NADH)… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 3039271 | Tanaka A, Morimoto T, Wakashiro S, Ikai I, Ozawa K, Orii Y: Kinetic alterations of cytochrome c oxidase in carbon tetrachloride induced cirrhotic rat liver. Life Sci. 1987 Aug 10;41(6):741-8. However, when the rate of uptake by mitochondria was measured in the presence of rotenone and tetramethyl-p-phenylene-diamine with as substrate, the specific activity in CCl4 treated rats was lower than that of normal rats (Vmax = 345 +/- 31 (e-/s/cytochrome aa3), as compared to Vmax = 408 +/- 21) in spite of the increased activity of cytochrome c oxidase. This phenomenon was ascribed to a decrease in the activity of NADH cytochrome b5 reductase in the mitochondrial outer membrane due to CCl4 treatment. |
1(0,0,0,1) | Details |
| 167532 | Bartoli GM, Dani A, Galeotti T, Russo M, Terranova T: Respiratory activity of Ehrlich ascites tumour cell nuclei. . Z Krebsforsch Klin Onkol Cancer Res Clin Oncol. 1975;83(3):223-31. Among the respiratory pigments analysed spectrophotometrically in the microsomal fraction prepared from ascites cells, only small amounts of flavoproteins (NADH-cytochrome b5 reductase and -cytochrome c reductase) were detectable. 3. |
1(0,0,0,1) | Details |
| 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 Besides, in the liver this compound is also capable of accepting electrons from NADH-cytochrome b5 reductase. |
1(0,0,0,1) | Details |
| 970953 | Prough RA, Imblum RL, Kouri RA: -cytochrome c reductase activity in cultured human lymphocytes. Arch Biochem Biophys. 1976 Sep;176(1):119-26. Similarity to the liver microsomal NADH-cytochrome b5 reductase and cytochrome b5 enzyme system. |
1(0,0,0,1) | Details |
| 7199109 | Il'chenko AP, Komarova GN: oxidation by the mitochondria of Torulopsis candida] . Mikrobiologiia. 1981 Nov-Dec;50(6):964-72. The cytochrome is reduced in aerobic conditions also in the presence of exogenous and rotenone. The results are indicative of the fact that different electron transport chains are involved in the transport of reducing equivalents from higher and aldehydes oxidized by mitochondria: in the first case, the --cytochrome b5 reductase chain, and in the second case, the main phosphorylating electron transport chain. |
1(0,0,0,1) | Details |
| 6802189 | Chistiakov VV, Pospelova LN: [Transport of electrons from mitochondria to microsomes in the reconstituted system of cell organelles]. Biokhimiia. 1982 Jan;47(1):55-61. The addition of (but not NAD+ and amytal (or rotenone) to the reconstituted system caused a 40-50% reduction of -reducible cytochrome P-450. |
0(0,0,0,0) | 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. |
0(0,0,0,0) | Details |
| 9500851 | Shimada H, Hirai K, Simamura E, Pan J: Mitochondrial -quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers. Arch Biochem Biophys. 1998 Mar 1;351(1):75-81. The outer membrane fractions, free from the contamination of inner membranes but with a few microsomes, catalyzed rotenone-insensitive but not oxidation by or PQ. |
0(0,0,0,0) | Details |
| 6265441 | Bernardi P, Azzone GF: Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes. J Biol Chem. 1981 Jul 25;256(14):7187-92. Addition of exogenous to rotenone- and antimycin A-treated mitochondria, in 125 mM KCl, results in rates of uptake of 0.5-1 and 10-12 nanoatoms of X mg protein-1 X min-1 in the absence and presence of cytochrome c, respectively. oxidation is blocked by mersalyl, an inhibitor of NADH-cytochrome b5 reductase. |
2(0,0,0,2) | Details |
| 9762923 | Bodrova ME, Dedukhova VI, Mokhova EN, Skulachev VP: Membrane potential generation coupled to oxidation of external in liver mitochondria. FEBS Lett. 1998 Sep 18;435(2-3):269-74. It is assumed that (i) hypotonic treatment or digitonin causes disruption of the outer mitochondrial membrane, and, as a consequence, desorption of the membrane-bound cytochrome c in a Mg2+-dependent fashion; (ii) incubation in isotonic KCI without Mg2+ results in swelling of mitochondrial matrix, disruption of the outer membrane and cytochrome c desorption whereas Mg2+ lowers the K+ permeability of the inner membrane and, hence, prevents swelling; (iii) desorbed cytochrome c is reduced by added via NADH-cytochrome b5 reductase and cytochrome b5 or by and is oxidized by cytochrome oxidase. Rotenone and myxothiazol do not inhibit delta psi generated by oxidation of exogenous |
1(0,0,0,1) | Details |
| 7358642 | Ito A: Cytochrome b5-like hemoprotein of outer mitochondrial membrane: OM cytochrome b. J Biochem. 1980 Jan;87(1):73-80. Contribution of OM cytochrome b to rotenone-insensitive -cytochrome c reductase activity.. The specificity of each antibody was confirmed by inhibition studies of -cytochrome c reductase activities reconstituted from purified cytochromes and NADH-cytochrome b5 reductase. |
1(0,0,0,1) | Details |
| 6275889 | Bernardi P, Azzone GF: ATP synthesis during exogenous oxidation. Biochim Biophys Acta. 1982 Jan 20;679(1):19-27. oxidation, both in intact and in water-treated mitochondria, is 90% inhibited by mersalyl, an inhibitor of the outer membrane NADH-cytochrome b5 reductase, and 10% inhibited by rotenone. |
82(1,1,1,2) | Details |
| 532525 | Takaishi M, Shimizu T, Shishiba Y: Solubilization of -5'-deiodinase activity from rat liver microsome fraction. Acta Endocrinol. 1979 Dec;92(4):694-701. The extent of solubilization was compared with that of protein, rotenone insensitive cytochrome c reductase or NADH cytochrome b5 reductase, which have been shown to associate with microsomal membrane rather than luminar contents. |
18(0,0,3,3) | Details |
| 8192914 | Birch-Machin MA, Briggs HL, Saborido AA, Bindoff LA, Turnbull DM: An evaluation of the measurement of the activities of complexes I-IV in the respiratory chain of human skeletal muscle mitochondria. Biochem Med Metab Biol. 1994 Feb;51(1):35-42. Complex I activity is measured in the presence of 2.5 mg.ml-1 bovine serum albumin, which increases rotenone sensitivity, and we have shown that NADH-cytochrome b5 reductase makes an important contribution to the rotenone-insensitive NADH-ubiquinone oxidoreductase activity. |
6(0,0,1,1) | Details |
| 7391131 | Borgese N, Meldolesi J: Localization and biosynthesis of NADH-cytochrome b5 reductase, an integral membrane protein, in rat liver cells. J Cell Biol. 1980 Jun;85(3):501-15. In fresh heavy and light Golgi fractions (GF3 and GF1 + 2) and in mitochondria, the specific activity of rotenone-insensitive -cytochrome c reductase was approximately 100, 60, and 30%, respectively, of the value found in microsomes. |
3(0,0,0,3) | Details |