α3β3 complex of thermophilic ATP synthase Catalysis without the γ‐subunit

FEBS Letters

Kagawa, Yasuo¹  Otawara-Hamamoto, Yoko¹  Ohta, Shigeo¹ 

[1] Department of Biochemistry, Jichi Medical School, Minamikawachi-machi, Tochigi-ken, 329-04, Japan

关键词: F1-ATPase;    Oligomer;    α3β3;    ATPase;    ATP synthesis;    (Thermophilic bacteria);    F1;    catalytic portion of ATP synthase;    TF1;    F1 from thermophilic bacterium PS3;    EF1;    F1 from E. coli;    AMPPNP;    adenyl-5′-yl imidodiphosphate;    DMSO;    dimethyl sulfoxide;    DTT;    dithiothreitol;    Mes;    4-morpholineethanesulfonic acid;    α;    β and γ;    subunits of F1;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(89)80017-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A complex of the α- and β-subunits of thermophilic ATP synthase showed about 25% of the ATPase activity of the αβγ complex. The α₃β₃ hexamer structure was analyzed by sedimentation (11.2 S) and gel filtration (310 kDa). Dilution of the αβ complex caused dissociation of the complex and rapid loss of ATPase activity which was restored by addition of the γ-subunit. A previous method using urea for isolating the subunits resulted in an αβ complex with lower activity than that prepared by over-expression of the genes. The αβ-ATP complex was formed from the αβ complex, ADP and P_i in the presence of dimethyl sulfoxide.

【 授权许可】

Unknown