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• W1484840173 abstract "The effects of digitonin and tocopherol on bovine heart reduced diphosphopyridine nucleotide- and succinate-cytochrome c reductases and cytochrome c oxidase have been studied with the following results. 1. Low concentrations of digitonin stimulate succinate- and DPNH-cytochrome c reductase and cytochrome c oxidase. Higher concentrations of digitonin completely inhibit cytochrome c reductases, while continuing to stimulate cytochrome c oxidases. 2. Inhibition of the reductases is reversed by either dilution or addition of tocopherol. Stimulation of the reductases and oxidase is prevented by tocopherols but is not reversed by either tocopherols or dilution. 3. Of other compounds tested for ability to prevent these digitonin effects, α-tocopherol polyethylene glycol succinate 1000 and coenzyme Q4 chromanol were effective with a soluble preparation of DPNH-cytochrome c reductase. In addition to these, α-tocopheryl succinate and α-tocopheryl phosphate were effective with a particulate preparation of succinate-cytochrome c reductase. α-Tocopheryl succinate, α-tocopheryl phosphate, α-tocopheryl hydroquinone, and vitamin D2 prevented the stimulation of cytochrome c oxidase. 4. Digitonin stimulation of succinate-cytochrome c reductase is associated with increases in both Vmax and Km (succinate); digitonin inhibition is associated with decreases in both Vmax and Km (succinate). 5. Reduced with respect to oxidized difference spectra of normal and inhibited preparations indicated succinate reduction of cytochromes a + a3, b, and c1, and of flavin in the normal enzyme, but almost no reduction of flavin and cytochromes of a digitonin-inhibited enzyme. 6. Digitonin caused almost complete inhibition of enzymatic reduction of ferricyanide by succinate, but only partial inhibition of reduction of indophenol and phenazine methosulfate. It is concluded from this and from the spectral studies that inhibition is before cytochrome b and after, or at, the flavin. 7. Digitonin stimulates both the reduction or oxidation of cytochrome c but not the reduction of ferricyanide. It is concluded that stimulation is due to irreversible changes in the enzyme that permit more rapid reaction of soluble cytochrome c with the particulate enzyme. 8. Tocopherol apparently forms an insoluble complex with digitonin and decreases the concentration of digitonin in solution. This is possibly the mechanism by which tocopherol counteracts the effects of digitonin on enzymes. Other compounds known to combine with digitonin do not decrease the concentration of digitonin under the conditions of the enzyme assays." @default.
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• W1484840173 date "1966-04-01" @default.
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• W1484840173 title "Effects of Digitonin and Tocopherol on Bovine Heart Muscle Reduced Diphosphopyridine Nucleotide- and Succinate-Cytochrome c Reductase and Cytochrome c Oxidase" @default.
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• W1484840173 doi "https://doi.org/10.1016/s0021-9258(18)96757-8" @default.
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