INFLUENCE OF MUTATION IN ε SUBUNIT OF Escherichia coli H~+-ATPase COMPLEX (F1F0) ON BIOCHEMICAL PROPERTIES OF THE ENZYME

The membrane-bound H~+-ATPase of E. coil consisted of two parts: Fand F. Purified ε subunit of Fstrongly inhibited Fbut showed no inhibitory effect in reconstituted FF. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that FFcomplex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the mutant