Abstract
The cation-complexing carboxylic-acid antibiotic X-537A, at concentrations far below that required for ionophorous activity, selectively inhibits the oxidation of glutamate and isocitrate by liver mitochondria in steady-state 3. The site of inhibition has been localized specifically at the reduction of NADP+. Glutamate and isocitrate dehydrogenases, the oxidation of NAD+-dependent substrates, pyridine nucleotide transhydrogenations, and the respiratory chain between NADH (or NADPH) and O2 are unaffected by the antibiotic X-537A. Kinetic evidence, i.e., competition between chlorotetracycline (a fluorescence probe for membrane-bound bivalent cation) and X-537A, indicates that the NADP+-reducing, antibiotic-sensitive site is most probably associated with the inner mitochondrial membrane.
Keywords: antibiotic X-537A, chlorotetracycline, membrane
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