| Name | cytochrome b 5 |
|---|---|
| Synonyms | CYB 5; CYB5; CYB5A; Cytochrome b 5; Cytochrome b5; MCB 5; MCB5; Microsomal cytochrome b5… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 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. During oxidation of exogenous there is a fast and complete reduction of cytochrome b5 while endogenous or added exogenous cytochrome c become 10-15% and 100% reduced, respectively. |
3(0,0,0,3) | Details |
| 856833 | Jarasch ED, Bruder G, Keenan TW, Franke WW: Redox constituents in milk fat globule membranes and rough endoplasmic reticulum from lactating mammary gland. J Cell Biol. 1977 Apr;73(1):223-41. Both fractions contained significant amounts of a b-type cytochrome with several properties similar to those of cytochrome b5 from liver, as well as a rotenone-insensitive - and -cytochrome c reductase. |
8(0,0,1,3) | Details |
| 7358642 | Ito A: Cytochrome b5-like hemoprotein of outer mitochondrial membrane: OM cytochrome b. J Biochem. 1980 Jan;87(1):73-80. The participation of OM cytochrome b in the rotenone-insensitive -cytochrome c reductase activity of rat tissues was investigated in comparison with that of cytochrome b5, by using antibodies against these two cytochromes. |
8(0,0,1,3) | Details |
| 7306601 | Lemeshko VV: [Effect of on the cytochrome c reductase activity of microsomes and outer mitochondrial membrane of rat liver depending on age]. Biokhimiia. 1981 Oct;46(10):1807-14. The rotenone-insensitive -cytochrome c reductase activity and cytochrome b5 content in mitochondria and microsomes of liver of 1-, 3-, 12- and 24-month-old rats were studied. |
7(0,0,1,2) | Details |
| 6742854 | Yoshida S, Yubisui T, Takeshita M: Characteristics of b-type cytochromes in brain microsomes: comparison with liver microsomes. Arch Biochem Biophys. 1984 Jul;232(1):296-304. Biochemical aspects of b-type cytochromes in swine cerebral microsomes were different from those of cytochrome b5 in liver microsomes, as well as the difference in absorption spectra. First, the kinetic constants, Km and Vmax, in rotenone-insensitive -cytochrome c reductase activity were different from those of liver microsomes, and the activity of cerebral microsomes was higher than that of liver microsomes. |
3(0,0,0,3) | 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. It was concluded that the electron transfer from the NAD-dependent substrates of the inner mitochondrial respiratory chain to the microsomal cytochrome P-450 occurs with the participation of non-bound NAD and cytochrome b5 of the outer mitochondrial membrane on the condition that the membranes of the two main oxidative systems are in tight contact. |
1(0,0,0,1) | Details |
| 4393016 | Kamino K, Inouye A: Light-scattering studies on rabbit brain microsomes. 3. Biochim Biophys Acta. 1970;205(2):246-53. Coupling of cytochrome b5 and related oxidative activities with microsomal contraction. |
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. These nuclei contain cytochrome b5, whereas cytochrome P-450 or mitochondrial-like cytochromes are lacking. 4. |
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 |
| 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 |
| 468787 | Keyes SR, Alfano JA, Jansson I, Cinti DL: Rat liver microsomal elongation of fatty acids. J Biol Chem. 1979 Aug 25;254(16):7778-84. Possible involvement of cytochrome b5. |
1(0,0,0,1) | Details |
| 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. A variety of electron acceptors have been compared as to rate with the following result: ferricyanide greater than cytochrome c greater than cytochrome b5 greater than greater than dichlorophenolindophenol. |
1(0,0,0,1) | Details |
| 10781794 | Lemeshko VV: Mg (2+) induces intermembrane electron transport by cytochrome c desorption in mitochondria with the ruptured outer membrane. FEBS Lett. 2000 Apr 21;472(1):5-8. We showed that Mg (2+) significantly stimulated IMET insensitive to rotenone-antimycin A-myxothiazol in mitochondria with the hypotonically damaged outer membrane, even in the absence of exogenous cytochrome c. Obtained data suggest that cytochrome b (5) is normally oriented towards the cytosol in the outer membrane, and can be accessible for endogenous cytochrome c reduction only through the outer membrane rupture or permeabilization, to activate external oxidation. |
1(0,0,0,1) | 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 contrast to their behavior in microsomes, the distribution of -cytochrome c reductase and cytochrome b5 of Golgi fractions was shifted by digitonin, although to a lesser extent than that of galactosyl transferase. 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. |
1(0,0,0,1) | Details |
| 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. The enzyme showed greatest electron acceptor activity with ferricyanide (100%), followed by cytochrome c (3.5%), dichloroindophenol (2.7%), and cytochrome b5 (0.34%). |
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. It is concluded that (i) oxidation of exogenous in the presence of cytochrome c proceeds mostly through NADH-cytochrome b5 reductase and cytochrome b5 on the outer membrane and then through cytochrome oxidase via the cytochrome c shuttle, and (ii) ATP synthesis during oxidation of exogenous is partly due to oxidation of endogenous substrates and partly to operation of cytochrome oxidase receiving electrons from the outer membrane via cytochrome c. 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. |
1(0,0,0,1) | Details |