作者: Mauro DEGLI ESPOSTI , Ah-Lim TSAI , Graham PALMER , Giorgio LENAZ
DOI: 10.1111/J.1432-1033.1986.TB10073.X
关键词:
摘要: We have investigated the oxidation of reduced ubiquinol: cytochrome c (bc1 complex) isolated from beef heart mitochondria. The c1 by both potassium ferricyanide and in ascorbate-reduced bc1 complex is not a first-order process. This taken as evidence that rapid equilibrium with Rieske iron-sulphur center. Among several inhibitors tested, only 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole stigmatellin are seen to affect this redox between high-potential centers complex. The b succinate-reduced fully blocked all tested. inhibition occurs simultaneoulsy an acceleration c1, even after extraction endogenous ubiquinone which present preparation. Almost complete has no effect upon phase oxidation, nor does it alter various inhibitors. The exogenous ubiquinones stimualted myxothiazol partially inhibited antimycin. However, addition these together completely blocks quinones. In contrast, simultaneous antimycin such synergistic c. Our data show intramolecular electron transfer cytochrome(s) center can take place without involvement ubiquinone-10. pathway sensitive enzyme.