The maintenance of the energized membrane state and its relation to active transport in Escherichia coli.
1. An ATPase mutant of Escherichia coli and two partial revertants of that mutant were examined for the ability to generate a high energy membrane state with D-lactate or ATP, as measured by the quenching of the fluorescent dye quinacrine. 2. All three strains showed reductions in the aerobically-driven quenching of fluorescence compared to the wild type, but the reduction could be reversed by the addition of eitherN,N'-dicyclohexylcarbodiimide or the crude soluble ATPase of the wild type. 3. The mutant exhibited a decreased ability to accumulate sugars and amino acids and showed an increased permeability to protons. 4. One partial revertant showed a slight increase in active transport and a slight decrease in proton permeability. 5. The other partial revertant showed a large increase in transport ability and a large decrease in proton permeability. 6. A model is proposed in which the conformation of the Mg-2+-ATPase is important in the utilization of energy derived from the electron transport chain and this function is independent of the catalytic activity of the Mg-2+-ATPase.
D000251:Adenosine Triphosphatases; D000255:Adenosine Triphosphate / Q000378:metabolism; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism*; D004735:Energy Transfer; D004926:Escherichia coli / Q000378:metabolism*; D007773:Lactates / Q000378:metabolism; D008954:Models, Biological; D009154:Mutation; D013045:Species Specificity; D013050:Spectrometry, Fluorescence
D007773:Lactates; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases