Publication Cover
Redox Report
Communications in Free Radical Research
Volume 7, 2002 - Issue 2
200
Views
2
CrossRef citations to date
0
Altmetric
Research Articles

Yeast thioredoxin peroxidase expression enhances the resistance of Escherichia coli to oxidative stress induced by singlet oxygen

, &
Pages 79-84 | Published online: 19 Jul 2013

  • Kanofsky JR. Singlet oxygen production by biological systems. Chem Biol Interact 1989; 70: 1–28.
  • Weishaupt KR, Gomer CJ, Dougherty TJ. Identification of singlet oxygen as the cytotoxic agent in photoinactivaticn of a murine tumor. Cancer Res 1976;36: 2326–2329.
  • Halliwell B, Gutteridge JMC. Free Radicals in Biology and Medicine, Oxford: Oxford University Press, 1999.
  • McCord JM, Fridovich I. Superoxide dismutase, an enzyme function of erythrocuprein. J Biol Chem 1969;224: 6049–6055.
  • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mam-malian organs. Physiol Rev 1979; 59: 527–605.
  • Cerutti PA. Prooxidant states and tumor promotion. Science 1985; 227:375–380.
  • Kim K, Kim IR, Lee KY, Rhee SG, Stadtman ER. The isolation and purification of a specific ‘protector’ protein which inhibits enzyme inactivation by a thiol/Fe(11)/02 mixed-function system. J Biol Chem 1988;263: 4704–4711.
  • Kim IR, Kim K, Rhee SG. Induction of an antioxidant protein of Sacchammyces cerevisiae by 02, Fe', or 2-mercaptoethanol. Proc Natl Acad Sci USA 1989;86: 6018–6022.
  • Kwon SJ, Park JW, Kim K. Inhibition of metal-catalyzed oxidation system by a yeast protector protein in the presence of thiol. Biochem Mol Biol Int 1994;32: 419–427.
  • Kwon SJ, Park JW, Choi WK, Kim IR, Kim K. Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the pre-sence of thioredoxin. Biochem Biophys Res Commun 1994;201: 8–15.
  • Chae FE, Chung SJ, Rhee SG. Thioredoxin-dependcnt peroxide reductase from yeast. J Biol Chem 1994; 269: 27670–27678.
  • Lee SM, Park JW. A yeast mutant lacking thiol-dependent protector protein is hypersensitive to menadione. Biochim Biophys Acta 1998; 1382: 167–175.
  • Chae FE, Kim IR, Kim K, Rhee SG. Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Sacchatomyces cerevisiae. J Biol Chem 1993; 268: 16815-16821.
  • Tabatabaie T, Floyd RA. Susceptibility of glutathioneperoxidase and glutathionereductase to oxidative damage and the protective effect of spin trapping agents. Arch Biochem Biophys 1994; 314: 112–119.
  • Ahn SM, Lee SM, Chung TW, Kim K, Park JW. Yeast thiol-dependent protector protein expression enhances the resistance of Escherichia coli to hydrogen peroxide. Biochem Mol Biol Int 1996; 39: 1007–1015.
  • Levine RL, Williams JA, Stadtman ER, Shacter E. Carbonyl assays for determination of wddatively modified proteins. Methods Enzymol 1994; 233: 346–357.
  • Beuge S, Aust S. Microsomal lipid peroxidation. Methods Enzymol 1978; 52: 302–310.
  • Beers Jr RF, Sizer IW. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 1952; 195: 33–40.
  • Marklund SL, Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 1974; 47:469–474.
  • Beauchamp C, Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 1971; 44: 276–287.
  • Amici A, Levine RL, Tsai L, Stadtman ER. Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. J Biol Chem 1989; 264: 3341–3346.
  • Sies H. Biochemistry of oxidative stress. Angew Chem Int Edn Engl 1986; 25: 1058–1072.
  • Krinsky NI. Membrane photochemistry and photobiology Photochem Photobiol1974; 20: 532-535.
  • Pyror WA. (ed) Free Radicals in Biology, vol 2. New York: Academic Press, 1977; 85-133.
  • Joshi PC. Comparison of the DNA-damaging property of photosensitised riboflavin via singlet oxygen (102) and superoxide radical O. Mechanisms. Toxicol Lett 1985; 26: 211–217.
  • de Mol NJ, van Henegouven GMJB, van Beele B. Singlet oxygen formation by sensitization of furocoumarins complexed with, or bound covalently to DNA. Photochem Photobiol1981; 34: 661-666.
  • Hasan T, Khan AU. Phototoxicity of the tetracyclines: photosensitized emission of singlet delta dioxygen. Proc Natl Acad Sci USA 1986; 83: 4604–4606.
  • Mathews-Roth MM. Beta-carotene therapy for erythropoietic protoporphyriaand other photosensitivity diseases. Biochimie 1986; 68: 875–884.
  • Egorov SL Babizhaev MA, Krasnovskii Jr AA, Shredova AA. Photosensitized generation of singlet molecular oxygen by endogenous substances of the eye lens. Biofizika 1987; 32: 169–171.
  • Lim YS, Cha MK, Kim HK et al. Removal of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo. Biochem Biophys Res Commun 1993; 192: 273–280.
  • Kono Y, Fridovich I. Superoxide radical inhibits catalase. J Biol Chem 1982;257: 5751–5754.
  • Christman MF, Morgan RW, Jacobson FS, Ames BN. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 1985; 41:753–762.
  • Greenberg JT, Monach P, Chou JH, Josephy PD, Demple B. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci USA 1990; 87: 6181-6185.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.