title: Changes in the proton-motive force in Escherichia coli in response to external oxidoreduction potential.
abstract: The pH homeostasis and proton-motive force (Deltap) of Escherichia coli are dependent on the surrounding oxidoreduction potential (ORP). Only the internal pH value and, thus, the membrane pH gradient (DeltapH) component of the Deltap is modified, while the membrane potential (DeltaPsi) does not change in a significant way. Under reducing conditions (Eh < 50 mV at pH 7.0), E. coli decreases its Deltap especially in acidic media (21% decrease at pH 7.0 and 48% at pH 5.0 for a 850-mV ORP decrease). Measurements of ATPase activity and membrane proton conductance (CH+m) depending on ORP and pH have shown that the internal pH decrease is due to an increase in membrane proton permeability without any modification of ATPase activity. We propose that low ORP values de-energize E. coli by modifying the thiol : disulfide balance of proteins, which leads to an increase in the membrane permeability to protons.
authors.affiliation: Laboratoire de Microbiologie U.A. INRA, ENSBANA, Université de Bourgogne, Dijon, France.
authors.forename: C
authors.initials: C
authors.lastname: Riondet
authors.forename: R
authors.initials: R
authors.lastname: Cachon
authors.forename: Y
authors.initials: Y
authors.lastname: Waché
authors.forename: G
authors.initials: G
authors.lastname: Alcaraz
authors.forename: C
authors.initials: C
authors.lastname: Diviès
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials; D010084:Oxidation-Reduction; D011522:Protons
chemical_list: D011522:Protons; D000251:Adenosine Triphosphatases