On the site of action of the inhibition of the mitochondrial respiratory chain by lipoxygenase.
Treatment of beef-heart submitochondrial particles with reticulocyte lipoxygenases gives rise to a strong irreversible inhibition of the NADH and succinate oxidase activities. This is not accompanied by any loss of the Fe-S clusters of the respiratory chain as determined by EPR spectroscopy. The inhibitory blockage is located between both the NADH and succinate dehydrogenases and Q-10. The inhibitory action of treatment with lipoxygenase also takes place in the absence of Q-10. The Fe-S clusters of the mitochondrial outer membrane are destroyed by lipoxygenase treatment, without any effect on the rotenone-insensitive NADH: cytochrome c oxidoreductase activity. It is concluded that these clusters are not involved in this enzyme.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport / Q000187:drug effects; D008084:Lipoxygenase / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000378:metabolism*; D016660:NAD(P)H Dehydrogenase (Quinone); D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors*; D011808:Quinone Reductases / Q000037:antagonists & inhibitors*; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology*; D013367:Submitochondrial Particles / Q000201:enzymology / Q000378:metabolism*; D014451:Ubiquinone / Q000378:metabolism
D014451:Ubiquinone; D008084:Lipoxygenase; D009247:NADH, NADPH Oxidoreductases; D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases