2 BINDING-SITES OF INHIBITORS IN NADH-UBIQUINONE OXIDOREDUCTASE (COMPLEX-I) - RELATIONSHIP OF ONE-SITE WITH THE UBIQUINONE-BINDING SITE OF BACTERIAL GLUCOSE-UBIQUINONE OXIDOREDUCTASE
2 BINDING-SITES OF INHIBITORS IN NADH-UBIQUINONE OXIDOREDUCTASE (COMPLEX-I) - RELATIONSHIP OF ONE-SITE WITH THE UBIQUINONE-BINDING SITE OF BACTERIAL GLUCOSE-UBIQUINONE OXIDOREDUCTASE
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DOI：
10.1111/j.1432-1033.1994.tb19985.x
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发表时间：
1994-01-15
期刊：
影响因子：
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通讯作者：
WEISS, H
中科院分区：
文献类型：
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作者：
FRIEDRICH, T;VANHEEK, P;WEISS, H
研究了10种天然存在的和两种合成的NADH抑制剂：牛心、粗糙脉孢菌和大肠杆菌的辅酶Q氧化还原酶（复合物I）和葡萄糖氧化酶的葡萄糖：辅酶Q氧化还原酶（葡萄糖脱氢酶）的作用。这些抑制剂可根据其特异性和作用方式分为两类。I类抑制剂，包括天然存在的杀粉蝶菌素A、番荔枝素VI、非那酰胺A（2）、aurachins A和B、噻昂唑和合成的唑螨酯，以部分竞争性方式抑制来自所有三个物种的复合物I，并以竞争性方式抑制葡萄糖脱氢酶，两者都与泛醌有关。II类抑制剂包括天然存在的鱼藤酮、吩恶生、aureothin和合成的苯并咪唑以非竞争性方式抑制来自所有物种的复合物I，但对葡萄糖脱氢酶没有影响。Myxalamid PI不能如上分类，因为它仅以竞争方式抑制线粒体复合物I。所有的抑制剂影响电子转移步骤从高电位的铁硫簇泛醌。I类抑制剂似乎直接作用于与复合物I和葡萄糖脱氢酶相关的泛醌催化位点。
The effect of ten naturally occurring and two synthetic inhibitors of NADH:ubiquinone oxidoreductase (complex I) of bovine heart, Neurospora crassa and Escherichia coli and glucose:ubiquinone oxidoreductase (glucose 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 A(2), aurachins A and B, thiangazole and the synthetic fenpyroximate, inhibit complex I 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.