Evidence that 4‐azido‐2‐nitrophenylphosphate binds to the phosphate site on the β‐subunit of Escherichia coli BF1‐ATPase

FEBS Letters

Pougeois, Richard¹  Vignais, Pierre V.¹  Lauquin, Guy J.-M.¹ 

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

关键词: Bacterial ATPase;    Phosphate binding site;    Photoaffinity;    4-Azido-2-nitrophenylphosphate;    Pi;    inorganic phosphate;    MF1;    mitochondrial ATPase;    BF1;    E. coli ATPase;    TF1;    ATPase isolated from the thermophilic bacterium PS3;    CF1;    chloroplast F1;    ANP;    4-azido-2-nitrophenol;    ANPP;    4-azido-2-nitrophenylphosphate;    TMMg;    50 mM Tris;    50 mM MES;    1 mM MgSO4 (pH 7.5);    TMES;    50 mM Tris;    50 mM MES;    1 mM EDTA;    1 mM Na2SO4 (pH 7.5);    NEM;    N-ethylmaleimide;    DCCD;    N;    N′-dicyclohexylcarbodiimide;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(83)80120-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The P_i binding site on bacterial ATPases, isolated from Escherichia coli and from the thermophilic bacterium PS3, was located by means of radiolabeled 4-azido-2-nitrophenylphosphate (ANPP), a photoaffinity derivatives of P_i. Complete inactivation of both ATPases required 1 mol [³²P]ANPP/mol ATPase. Only the β-subunit was photolabeled.

【 授权许可】

Unknown