Inhibition of membrane-bound succinate dehydrogenase by fluorescamine.
Fluorescamine rapidly inactivated membrane-bound succinate dehydrogenase. The inhibition of the enzyme by this reagent was prevented by succinate and malonate, suggesting that the group modified by fluorescamine was located at the active site. The modification of the active site sulfhydryl group by 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) did not alter the inhibitory action of fluorescamine. However, the protective effect of malonate against fluorescamine inhibition was abolished in the enzyme modified at the thiol.
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Departamento de Bioquimica, Instituto Nacional de Cardiologia, Ignacio Chavez, Mexico, D.F.
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Garcia
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D000818:Animals; D002417:Cattle; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology; D005450:Fluorescamine / Q000494:pharmacology*; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D008314:Malonates / Q000494:pharmacology; D008929:Mitochondria, Heart / Q000201:enzymology*; D011485:Protein Binding; D013367:Submitochondrial Particles / Q000201:enzymology*; D013385:Succinate Dehydrogenase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013386:Succinates / Q000494:pharmacology; D019802:Succinic Acid
D008314:Malonates; D013386:Succinates; D005450:Fluorescamine; D004228:Dithionitrobenzoic Acid; C030290:malonic acid; D019802:Succinic Acid; D013385:Succinate Dehydrogenase