Changes in the proton-motive force in Escherichia coli in response to external oxidoreduction potential

European Journal of Biochemistry

Volumn 262, Issue 2, 1999, Pages 595-599

  Riondet, Christophe ^a,b   Cachon, Rémy ^a,b   Waché, Yves ^a   Alcaraz, Gérard ^b   Diviès, Charles ^a  

^a UNIVERSITÉ DE BOURGOGNE   (France)

^b UNIVERSITÉ DE BOURGOGNE   (France)

Author keywords

Escherichia coli; Membrane potential; Oxidoreduction potential; Protomotive force; Proton membrane conductance

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ARTICLE; ENZYME ACTIVITY; ESCHERICHIA COLI; MEMBRANE CONDUCTANCE; MEMBRANE PERMEABILITY; MEMBRANE POTENTIAL; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PH; PRIORITY JOURNAL; PROTON MOTIVE FORCE; PROTON TRANSPORT;

ADENOSINE TRIPHOSPHATASES; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MEMBRANE POTENTIALS; OXIDATION-REDUCTION; PROTONS;

EID: 0033152799     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00429.x     Document Type: Article

References (37)

1. 1. Ingraham, J.L. & Marr, A.G. (1996) Effect of temperature, pressure, pH and osmotic stress on growth. In Escherichia coli and Salmonella (Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. & Umbarger, H.E., eds), pp. 1570-1578, ASM Press, Washington DC, USA.
2. 2. Reed, G.B. & Orr, J.H. (1943) Cultivation of anaerobes and oxidation-reduction potentials. J. Bacterial. 45, 309-320.
3. 3. Oblinger, J.L. & Kraft, A.A. (1973) Oxidation-reduction potential and growth of Salmonella and Pseudomonas fluorescens. J. food Sci. 38, 1108-1112.
4. 4. Pearson, C.B. & Walker, H.W. (1976) Effect of oxidation-reduction potential upon growth and sporulation of Clastridium perfringens. J. Milk Food Tecknol. 39, 421-425.
5. 5. Futter, B.V. & Richardson, G. (1970) Viability of clostridial spores and the requirements of damaged organisms. J. Appl. Bact. 33, 331-341.
6. 6. Reichart, O. & Szakmar, K. (1988) The effect of redox potential on the thermal death of microorganisms. Elelmezési Ipar 43, 142-146.
7. 7. Szakmar, K., .Reichart, O. & Vineze, L. (1988) The effect of redox potential on the thermal death of microorganisms II. Elelmezési Ipar 42, 281-285.
8. 8. Winpenny, J.W.T. & Necklen, D.K. (1971) The redox environment and microbial physiology. Biochim. Biophysic. Acta 253, 352-359.
9. 9. Javor, G.T. & Febre, E.F. (1992) Enzymatic basis of thiol-stimulated secretion of porphyrins by Escherichia coli. J. Bacteriol. 174, 1072-1075.
10. 10. Kwong, S.C.W. & Rao, G. (1991) Utility of culture redox potential for identifying state changes in amino acid fermentation. Biotechnol. Bioeng. 38, 1034-1040.
11. 11. Unden, G., Trageser, M. & Duchêne, A. (1990) Effect of positive redox potentials (>+400mV) on the expression of anaerobic respiratory enzymes in Escherichia coli. Mol. Microbiol. 4, 315-319.
12. 12. Bespalov, V.A., Zhulin, I.B. & Taylor, B.L. (1996) Behavioral responses of Escherichia coli to changes in redox potential. Proc. Natl Acad. Sci. USA 93, 10084-10089.
13. 13. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randell, R.J. (1951) Protein measurement with the Polin phenol reagent. J. Biol. Chem. 193, 265-275.
14. 14. Riondet, C, Cachon, R., Alcaraz, G. & Divies, C. (1997) Measurement of the intracellular pH in Escherichia coli with the internally conjugated probe 5-(and 6-) carboxyfluorescein succinimidyl ester. Biotechnol Tech. 11, 735-738.
15. 15. Kamo, N., Muratsugu, M., Hongoh, R. & Kobatake, Y. (1979) Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state. J Membrane Biol. 49, 105-121.
16. 16. Paulsen, I.T., Brown, M.H. & Skurray, R.A. (1996) Proton-dependent multidrug efflux systems. Microbiol. Rev. 60, 575-608.
17. 17. Szmelcman, S. & Adler, J. (1976) Change in membrane potential during bacterial chemotaxis. Proc. Natl Acad. Sci. USA 73, 4387-4391.
18. 18. Eisenbach, M. (1982) Changes in membrane potential of Escherichia coli in response to temporal gradients of chemicals. Biochemistry 21, 6818-6825.
19. 19. Lolkema, J.S., Hellingwerf, K.J. & Konings, W.N. (1982) The effects of probe binding on the quantitative determination of the proton-motive force in bacteria. Biochim. Biophys. Acta 681, 85-94.
20. 20. Lolkema, J.S., Abbing, A., Hellingwerf, K.J. & Konings, W.N. (1983) The transmembrane electrical potential in Rhodopseudomonas sphaeroides determined from the distribution of tetraphenyl-phosphonium after correction for its binding to cell components. J. Biochem. 130, 287-292.
21. 21. Zilberstein, D., Schuldiner, S. & Padan, E. (1979) Proton electrochemical gradient in Escherichia coli cells and its relation to active transport of lactose. Biochemistry 18, 669-673.
22. 22. Zilberstein, D., Agmon, V., Schuldiner, S. & Padan, E. (1984) Escherichia coli intracellular pH, membrane potential, and cell growth. J. Bacteriol. 158, 246-252.
23. 23. Tran, Q.H. & Unden, G. (1998) Change in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation. Eur. J. Biochem. 251, 538-543.
24. 24. Dufour, J.P., Amory, A. & Goffeau, A. (1988) Plasma membrane ATPase from the yeast Schizosaccharomyces pombe. Methods Enzymol. 157, 513-528.
25. 25. Rius, N., Solé, M., Francia, A. & Lorén, J.G. (1994) Buffering capacity of pigmented and non-pigmented strains of Serratia marcescens. Appl. Environ. Microbiol. 60, 2152-2154.
26. + conductance of lactic acid bacteria. FEMS Microbiol. Lett. 120, 291-296.
27. + conductance of Steptococcus lactis. J. Bacteriol. 140, 197-205.
28. 28. Felle, H., Porter, J.S., Slayman, C.L. & Kaback, H.R. (1980) Quantitative measurements of membrane potential in Escherichia coli. Biochemistry 19, 3585-3590.
29. + ATPases. Yeast 8, 589-598.
30. + membrane conductance of gram-negative bacteria. FEMS Microbiol. Lett. 130, 103-110.
31. 31. Andersen, C.L., Mattey-Dupraz, A., Missiakas, D. & Raina, S. (1997) A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/ DsbB ans DsbC redox proteins. Mol. Microbiol. 26, 121-132.
32. 32. van Iwaarden, PR., Driessen, A.J.M. & Konings, W.N. (1992) What we can learn from the effects of thiol reagents on transport proteins. Biochim. Biophys. Acta 1113, 161-170.
33. 33. Gill, R.T., Cha, H.J., Jain, A., Rao, G. & Bentley, W.E. (1998) Generating controlled reducing environments in aerobic recombinant Escherichia coli fermentations: effects on cell growth, oxygen uptake, heat shock protein expression, and in vivo CAT activity. Biotechnol. Bioeng. 59, 248-259.
34. 34. Missiakas, D. & Raina, S. (1997) Protein folding in the bacteria periplasm. J. Bacteriol. 179, 2465-2471.
35. 35. Konings, W.N. & Robillard, G.T. (1982) Physical mechanism for regulation of proton solute symport in Escherichia coli. Proc. Natl Acad. Sci. USA 79, 5480-5484.
36. 36. Robillard, G.T. & Konings, W.N. (1982) A hypothesis for the role of dithiol-disulfide interchange in solute transport and energy-transducing processes. Eur. J. Biochem. 127, 597-604.
37. + efflux controlled by the redox state of the cell. Arch. Microbiol. 154, 475-482.