INHIBITION OF OXIDATIVE PHOSPHORYLATION IN ESCHERICHIA COLI BY DIHYDROSTREPTOMYCIN

Publisher Website
Google Scholar
Abstract
Dihydrostreptomycin inhibited the oxidation of succinate in extracts of antibiotic-sensitive E. coli. The inhibitable reaction required both the particulate and the supernatant fractions from sonic extracts which had been centrifuged at 100,000 X g. Dihydrostreptomycin was found to inhibit phosphorylation coupled with the oxidation of reduced nicotinamide adenine dinu-cleotide (NADH). The inhibition of oxidative phosphorylation by dihydrostreptomycin appeared to precede the effect of the antibiotic on oxidation. The streptomycin antagonist, 2-heptyl-4-hydroxyquinoline N-oxide, inhibited the oxidation of succinate and of NADH, but showed little effect on oxidative phosphorylation. Oxidative phosphorylation was not affected by dihydrostreptomycin in strains of E. coli which were antibiotic-resistant or -dependent.