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. 1970 Jul;2(1):82–88. doi: 10.1128/iai.2.1.82-88.1970

Tirandamycin: Inhibition of Oxidative Phosphorylation in Rat Liver Mitochondria

Fritz Reusser 1
PMCID: PMC415968  PMID: 16557805

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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