EEDQ probably reacts with the Mg2+‐ATP catalytic sites of mitochondrial and bacterial F1‐ATPases
[摘要] The carboxyl reagent N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ) inactivated ATPase activities of isolated MF1 and BF1 when assayed in an MgCl2 medium, but not in an EDTA medium. However, another carboxyl reagent, N,N′-dicyclohexylcarbodiimide (DCCD) was found to inhibit MF1 and BF1 when assayed either in the presence of MgCl2 or EDTA. These data suggest that EEDQ interferes with the binding of Mg2+ at catalytic sites of both MF1 and BF1 and that EEDQ on one hand, and DCCD on the other, react with different carboxyl groups on MF1 and BF1.
[发布日期] [发布机构]
[效力级别] [学科分类] 生物化学/生物物理
[关键词] Mitochondrial ATPase;Bacterial ATPase;Carboxyl group;Catalytic site;N-Ethoxycarbonyl-2-ethoxy-1;2-dihydroquinoline;N;N′-Dicyclohexylcarbodiimide;MF1;beef heart mitochondrial ATPase;BF1;bacterial ATPase;TNP-ATP;2′;3′-O-(2;4;6-trinitrophenyl)-ATP;CMCD;1-cyclohexyl-3-(2-morpholino-4-ethyl)-carbodiimide;DCCD;N;N′-dicyclohexyl-carbodiimide;EEDQ;N-ethoxycarbonyl-2-ethoxy-1;2-dihydroquinoline;MOPS;3-(N-morpholino) propane sulfonic acid [时效性]
