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The mode of action of stigmatellin a new inhibitor of the cytochrome b c 1 segment of the respiratory chain



The mode of action of stigmatellin a new inhibitor of the cytochrome b c 1 segment of the respiratory chain



Biochimica et Biophysica Acta 765(2): 227-235



The new antibiotic stigmatellin, obtained from the myxobacterium Stigmatella aurantiaca, blocked electron flow in the respiratory chain of bovine heart submitochondrial particles [and Saccharomyces cerevisiae mitochondria] at the site of the cytochrome b-c1 segment. Its inhibitory potency was identical with that of antimycin and myxothiazol and, like these antibiotics, stigmatellin caused a shift in the spectrum of reduced cytochrome b. Difference spectroscopic studies with the 3 inhibitors in various combinations indicated that the binding site of stigmatellin was different from that of antimycin, but almost identical with that of myxothiazol. Experiments with 14 synthesized derivatives of stigmatellin showed that good inhibitory activity can be expected only if the side chain is relatively lipophilic, and the keto and the hydroxy groups of the chromone system are intact.

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