pH dependence of proton translocation by Escherichia coli

J Biol Chem. 1992 Jul 25;267(21):14559-62.

Abstract

Proton translocation in spheroplasts from Escherichia coli has been studied in two mutants, one of which expresses cytochrome o and the other cytochrome d as the terminal oxidase. Using the O2 pulse method, the H+/e- ratio of proton translocation associated with cytochrome o was confirmed to be near 2 at neutral pH, but was found to decrease considerably when the medium pH was raised above 8. At high pH there was an increase in H+/OH- permeability of the cell membrane, but this was not sufficient to explain the decline in proton ejection. The pH effect was confined to cytochrome o-linked activity. It was not present when cytochrome d generated the electrochemical proton gradient. This makes it improbable that the Na+/H+ antiporter is responsible. The most likely explanation for our finding is that there is a "slip" in the proton-pumping mechanism of cytochrome o at high pH.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytochrome b Group*
  • Cytochrome d Group
  • Cytochromes / metabolism
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Hydrogen-Ion Concentration
  • Oxygen / metabolism
  • Protons*
  • Spheroplasts / metabolism

Substances

  • Cytochrome b Group
  • Cytochromes
  • Escherichia coli Proteins
  • Protons
  • Cytochrome d Group
  • cytochrome bo, E coli
  • Oxygen