INFLUENCE OF MUTATION IN ε SUBUNIT OF Escherichia coli H^+-ATPase COMPLEX (F_1F_0) ON BIOCHEMICAL PROPERTIES OF THE ENZYME

作     者：吴季辉 林治焕 

作者机构：Institute of Biophysics Academia Sinica Beijing 100080 PRC Institute of Biophysics Academia Sinica Beijing 100080 PRC The membrane-bound H~+-ATPase of E. coil consisted of two parts: F_1 and F_0. Purified εsubunit of F_1 strongly inhibited F_1 but showed no inhibitory effect in reconstituted F_1F_0. In 1987 G. B. Cox et al. isolated a mutant of εsubunit and two partial revertants Their experiments showed that F_1F_0 complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the mutant 

出 版 物：《Chinese Science Bulletin》 (科学通报(英文版))

年 卷 期：1991年第36卷第5期

页      面：404-408页

学科分类：07[理学] 08[工学] 

基　　金：Project supported by the National Natural Science Foundation of China 

主　　题：Escherichia coli F₁F₀ εsubunit mutation. 

摘      要：The membrane-bound H+-ATPase of E. coil consisted of two parts: F1 and F0. Purified ε subunit of F1 strongly inhibited F1 but showed no inhibitory effect in reconstituted F1F0. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that F1F0 complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the