[The role of ATPase subunits from E. coli in hydrogen-potassium exchange].

A hypothesis was developed that in membranes of glycolysing bacteria functioned supercomplexes (F1 X F0-TrkA) and (F0-TrkA) which operated as H+-K+-pump exchanging 2H+ for one K+ and as H+-K+-antiport respectively. The mutants with defects in alpha, beta and gamma subunits of ATPase F1 manifested the alteration only in the work of (F1 X F0-TrkA). Defect in epsilon subunit of F1 broke the regulation of pump operation on the part of a cell turgor. In mutants with defects in F0 the changes in both supercomplexes were observed. The only mutation in unc- cluster producing the complete blocking of both systems operation was related to a defect in h3-subunit of F0 which was the dicyclohexylcarbodiimide-sensitive and apparently "gate" component of F0.