title: EEDQ probably reacts with the Mg2+-ATP catalytic sites of mitochondrial and bacterial F1-ATPases.
abstract: 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.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites / Q000187:drug effects; D002384:Catalysis; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology; D008274:Magnesium / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D011804:Quinolines / Q000494:pharmacology*
chemical_list: D001426:Bacterial Proteins; D011804:Quinolines; C000470:EEDQ; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D006180:Proton-Translocating ATPases; D008274:Magnesium