| Autor: |
Friedrich, Thornsten, Heek, Petra Van, Leif, Hans, Ohnishi, Tomoko, Forche, Edgar, Kunze, Brigitte, Jansen, Rolf, Trowitzsch-Kienast, Wolfram, Höfle, Gerhard, Reichenbach, Hans, Weiss, Hanns |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 1/15/94, Vol. 219 Issue 1/2, p691-698, 8p |
| Abstrakt: |
The effect of fen naturally occurring and two synthetic inhibitors of NADH:ubiquinone oxidoreductase (complex l) of bovine heart, Neurospora crassa and Escherichia coli and glucose:ubiquinone oxidoreductase (glucosc dehydrogenase) of Gluconobacter oxidans was investigated. These inhibitors could be divided into two classes with regard to their specifity and mode of action. Class I inhibitors, including the naturally occuring piericidin A, annonin VI, phenalamid A2, aurachins A and B, thiangazole and the synthetic fenpyroximate, inhibit complex ! from all three species in a partially competitive manner and glucose dehydrogenase in a competitive manner, both with regard to ubiquinone. Class II inhibitors including the naturally occuring rotenone, phenoxan, aureothin and the synthetic benzimidazole inhibit complex I from all species in an non-competitive manner; but have no effect on the glucose dehydrogenase. Myxalamid PI could not be classified as above because it inhibits only the mitochondrial complex I and in a competitive manner. All inhibitors affect the electron-transfer step from the high-potential iron-sulphur cluster to ubiquinone. Class I inhibitors appear to act directly at the ubiquinone-catalytic site which is related in complex I and glucose dehydrogenase. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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