Tirandamycin: Inhibition of Oxidative Phosphorylation in Rat Liver Mitochondria

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Tirandamycin inhibits respiration and phosphorylation in rat liver mitochondria. An investigation of individual reaction sequences occurring within the respiratory chain showed that the antibiotic stimulates reduced nicotinamide adenine dinucleotide (NADH)- and succinate-linked coenzyme Q reductase. NADH-linked reduction of tetrazolium salts remains unaffected by tirandamycin. Succinotetrazolium salt reductase is inhibited significantly. Reduction of cytochrome c by succinate is blocked by the antibiotic; NADH-cytochrome c reductase is inhibited but not completely blocked. Cytochrome c oxidase remains unaffected. Mitochondrial difference spectra prepared in the presence of tirandamycin indicate that the reduction of cytochrome b is not impaired but no reduction of cytochromes c or a is apparent. These results indicate that tirandamycin interferes with the respiratory chain at a point beyond the cytochrome b and prior to the cytochrome c reduction site. Tirandamycin acts also as a potent inhibitor of ribonucleic acid polymerase as discussed in the foregoing paper.

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