The noncatalytic site-deficient α3β3γ subcomplex and F0F1-ATP synthase can continuously catalyse ATP hydrolysis when Pi is present

被引:13
作者
Bald, D [1 ]
Muneyuki, E [1 ]
Amano, T [1 ]
Kruip, J [1 ]
Hisabori, T [1 ]
Yoshida, M [1 ]
机构
[1] Tokyo Inst Technol, Resources Utilizat Res Lab, Midori Ku, Yokohama, Kanagawa 226, Japan
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1999年 / 262卷 / 02期
关键词
ATP synthase; MgADP inhibited form; noncatalytic nucleotide binding sites; P-i;
D O I
10.1046/j.1432-1327.1999.00410.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We investigated ATP hydrolysis by a mutant (Delta NC) alpha(3)beta(3)gamma subcomplex of F0F1-ATP synthase from the thermophilic Bacillus PS3 that is defective in the noncatalytic nucleotide binding sites. This mutant subcomplex was activated by inorganic phosphate ions (P-i) and did not show continuous ATP hydrolysis activity in the absence of P-i. P-i also activated the wild-type alpha(3)beta(3)gamma subcomplex in a similar manner. Sulphate activated wild-type alpha(3)beta(3)gamma but not Delta NC alpha(3)beta(3)gamma, indicating that P-i activation did not involve noncatalytic sites but that sulphate activation did. P-i also activated ATP hydrolysis and coupled proton translocation by the wild-type and Delta NC F0F1-ATP synthases reconstituted into vesicle membranes.
引用
收藏
页码:563 / 568
页数:6
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