| 823748 |
Schewe T, Hiebsch C, Halangk W: [Action of the systemic fungicide dexon on several NADH dehydrogenases] . Acta Biol Med Ger. 1975;34(11-12):1767-75.
The fungicide dexon (p-dimethylaminobenzenediazosulfonate, Na-salt) inhibits the NADH oxidase activity of submitochondrial particles (ETP) from beef heart (semi-inhibition concentration 1.4 muM), while the succinate oxidase activity is unaffected. Measurements of the activity of several enzymatic partial reactions of the respiratory chain of ETP suggest that dexon acts directly on the flavine of NADH dehydrogenase. Soluble NADH-cytochrome c-oxidoreductase (MAHLER) and rotenone-insensitive NADH ubiquinone reductase are also inhibited by dexon. At low concentrations of dexon, inhibition of ETP starts slowly only after addition of NADH. Preincubation without NADH increases the amount of inhibition, but does not prevent the time delay. It is assumed that an electron flux through the respiratory chain, or reduction of flavine is prerequisite for the reaction of dexon with the action site. Furthermore, dexon inhibits the NADH dehydrogenase located at the outer surface of the inner membrane of plant mitochondria, accessible to extramitochondrial NADH and insensitive to rotenone, as has been shown on isolated mitochondria from cauliflower (Brassica oleracea L). In addition, dexon inhibits selectively the NADH dehydrogenase of the DT diaphorase (ERNSTER) from rat liver cytosol. In contrast, the dicoumarol-insensitive NADH dehydrogenase (ZINSMEYER et al.) from rat liver cytosol, the NADH-cytochrome b5-reductase (STRITTMATTER) from rat liver microsomes, the rotenone-insensitive NADH-cytochrome c-oxidoreductase of the outer membrane of rat liver mitochondria, soluble NADH-oxidase from Escherichia coli, and NADH-dehydrogenase from human erythrocytes are not inhibited. The results suggest that dexon is a group reagent to certain pyridine nucleotide-dependent flavine enzymes. |
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