EEDQ probably reacts with the Mg2+‐ATP catalytic sites of mitochondrial and bacterial F1‐ATPases

FEBS Letters

Pougeois, Richard¹ 

[1] Laboratoire de Biochimie (CNRS/ERA 903 et INSERM U.191), Département de Recherche Fondamentale, Centre d'Etudes Nucléaires, 85X, 38041 Grenoble cedex, France

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;   

DOI  :  10.1016/0014-5793(83)80872-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown