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Original Article

Glycerol metabolism in superoxide dismutase-deficient Escherichia coli

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Pages 867-872 | Received 26 Feb 2001, Published online: 07 Jul 2009

References

  • Lin E.C.C. Glycerol dissimilation and its regulation in bacteria. Annual Review in Microbiology 1976; 30: 535–578
  • Carlioz A., Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life?. EMBO Journal 1986; 5: 623–630
  • Imlay J.A., Fridovich I. Suppression of oxidative envelope damage by pseudoreversion of a superoxide dismutase-deficient mutant of Escherichia coli. Journal of Bacteriology 1992; 174: 953–961
  • Farr S.B., D'Ari R., Touati D. Oxygen-dependant mutagenesis in Escherichia coli lacking superoxide dismutase. Proceedings of the National Academy of Sciences of the United States of America 1986; 88: 8268–8273
  • Benov L., Fridovich I. A SOD mimic protects sodAsodB Escherichia coli against aerobic heating and stationary phase death. Archives of Biochemistry and Biophysics 1995; 322: 291–294
  • Zwaig N., Kistler W.S., Linn E.C.C. Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli. Journal of Bacteriology 1970; 102: 753–759
  • Maniatis T., Fritsch E.F., Sambrook J. Molecular Cloning. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 1982
  • Touati D., Jacques M., Tardat B., Bouchard L., Despied S. Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. Journal of Bacteriology 1995; 177: 2305–2314
  • Greenberg J.T., Monach P., Chou J.H., Josephy P.D., Demple B. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 1990; 87: 6181–6185
  • Tsaneva I.R., Weiss B. SoxR, a locus governing a superoxide response regulon in Escherichia coli K-12. Journal of Bacteriology 1990; 172: 4197–4205
  • Maringanti S., Imlay J. An intracellular iron chelator pleiotropically suppresses enzymatic and growth defects of superoxide dismutase-deficient Escherichia coli. Journal of Bacteriology 1999; 181: 3792–3802
  • Hayashi S., Lin E.C.C. Purification and properties of glycerol kinase from Escherichia coli. Journal of Biological Chemistry 1967; 212: 1030–1035
  • Freedberg W.B., Lin E. Three kinds of control affecting the expression of the glp regulon in Escherichia coli. Journal of Bacteriology 1973; 115: 816–823
  • Pettigrew W. Inactivation of Escherichia coli glycerol kinase by 5,5′-dithiobis (2-nitrobenzoic acid) and N-ethylmaleimide: evidence for nucleotide regulatory binding sites. Biochemistry 1986; 25: 4711–4718
  • Fliss H., Menard M. Oxidant-induced mobilization of zinc from metallothionein. Archives of Biochemistry and Biophysics 1992; 293: 195–199
  • Keyer K., Imlay J. Superoxide accelerates DNA damage by elevating free-iron levels. Proceedings of the National Academy of Sciences of the United States of America 1996; 93: 13635–13640
  • Davies K.J.A., Lin S.W. Degradation of oxidatively denatured proteins in Escherichia coli. Free Radical Biology and Medicine 1988; 5: 215–223
  • Davies K.J.A., Lin SW. Oxidatively denatured proteins are degraded by an ATP-indepenent proteolytic pathway in Escherichia coli. Free Radical Biology and Medicine 1988; 5: 215–223
  • Davies K.J.A. Protein damage and degradation by oxygen radicals. I. General aspects. Journal of Biological Chemistry 1987; 262: 9895–9901
  • Stadtman E.R. Oxidation of proteins by mixed-function oxidation system: implication in protein turnover, ageing and neutrophil function. Trends in Biochemical Sciences 1986; 11: 11–12
  • Wolf S.P., Dean R.T. Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymatic hydrolysis. Biochemical Journal 1986; 234: 399–403

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