The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<...The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<sub>1</sub> but showed no inhibitory effect in reconstituted F<sub>1</sub>F<sub>0</sub>. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that F<sub>1</sub>F<sub>0</sub> complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the展开更多
基金Project supported by the National Natural Science Foundation of China.
文摘The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<sub>1</sub> but showed no inhibitory effect in reconstituted F<sub>1</sub>F<sub>0</sub>. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that F<sub>1</sub>F<sub>0</sub> complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the