Journal of Bacteriology · 1984 · 101 citations · 16 references
Life SciencesBiologyMicrobiologyBacteriologyEnzymologyMicrobial PhysiologyAtp HydrolysisBacterial PhysiologyEnzyme KineticsMicrobial BioenergeticsPh ControlProton Motive ForceBacterial Proton Motive ForceMembrane AtpasesPh Effects On GrowthProton Motive Force RegulationProton Pump ActivityProton Pump FunctionProton Translocation MechanismsStreptococcus Species
When Streptococcus faecalis was grown in the presence of protonophores , an ATPase activity of the membrane was increased at a pH below 8.0 but not at a pH above 8.0. Characteristics of this increased ATPase were identical to those of a proton-translocating ATPase (H+-ATPase) located on the membrane of normal cells. The cytoplasmic pH was regulated at 7.6 to 7.8 but was not regulated in the presence of protonophores . The increase in the H+-ATPase was observed when the cytoplasmic pH was lowered to less than 7.6 by the addition of protonophores and was not related to the dissipation of the proton motive force. Thus, we suggest that the H+-ATPase of the membrane is amplified when the cytoplasmic pH is lowered below the pH at which it is regulated under normal conditions.
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Franklin M. Harold, E. Pavlasová, James R. Baarda · Biochimica et Biophysica Acta (BBA) - Biomembranes · 1970 · 182 citations
Constitutive Inorganic Pyrophosphatase of Escherichia coli
John Josse · Journal of Biological Chemistry · 1966 · 179 citations · Full text