| Abstract: | Two operation regimes of the electron transport system were found in rat liver mitochondria during the cyanide-resistant succinate oxidation catalyzed by menadione. Under isotonic conditions, the mitochondria were found to contain two electron transport components, one of which was sensitive to mucidin, whereas the other one was inhibited by antimycin A. Both electron transport components were inhibited by thenoyltrifluoroacetone (TTFA). In hypotonic media, the polyenzymatic respiratory complex of mitochondria underwent transformations. In this case the electron transport during the cyanide-resistant succinate oxidation was insensitive to mucidin and antimycin A and was suppressed only by TTFA. Some experimental evidence in favour of pathways of electron transfer under different regimes of mitochondrial function was obtained. It was supposed that in isotonic incubation media the cyanide-resistant respiration is mainly due to menadione reduction in two points of the Q-cycle, i.e., in the region of the "i" center and in the "o" center. Under hypotonic conditions, the main electron flux to menadione occurs only via the Q-cycle "i" center. The observed relatively slow reduction of cytochromes b and ci+c plays an insignificant role in the cyanide-resistant respiration. It was shown that the ability of menadione to stimulate the cyanide-resistant respiration is correlated with a higher polarity of this compound as compared with CoQ2 and endogenous CoQ10 of mitochondria. The role of the polyisoprenoid substituent in CoQ10 as a structural component providing for the specificity of interaction with mitochondrial respiratory chain carriers is discussed. |
