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How superoxide radical damages the cell

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Summary

Superoxide is considered to be poorly reactive, and cell damage has been attributed to HO· generated via the Haber-Weiss reaction. The function of O2 in this reaction is only to reduce Fe3+ to Fe2+. In vivo, however, superoxide could not out-compete cellular reductants such as glutathione, NADPH, and ascorbate, which makes the observed O2 toxicity rather puzzling. Little attention has been paid to the idea that, irrespective of its poor chemical reactivity, superoxide might be capable of interacting directly with specific intracellular targets; and that even the Haber-Weiss reaction might be a consequence of such direct interactions. This paper summarizes latest data that support the concept of such a mechanism.

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Abbreviations

SOD:

Superoxide dismutase

References

  • Benov L, Fridovich I (1995) A superoxide dismutase mimic protects sodAsodB Escherichia coli against aerobic heating and stationary-phase death. Arch Biochem Biophys 322: 291–294

    Google Scholar 

  • — — (1996) The rate of adaptive mutagenesis in Escherichia coli is enhanced by oxygen (superoxide). Mutat Res 357: 231–236

    Google Scholar 

  • — — (1997) Superoxide imposes leakage of sulfite from Escherichia coli. Arch Biochem Biophys 347: 271–274

    Google Scholar 

  • — — (1999) Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli. J Biol Chem 12: 4202–4206

    Google Scholar 

  • —, Kredich NM, Fridovich I (1996) The mechanism of the auxotrophy for sulfur-containing amino acids imposed upon Escherichia coli by superoxide. J Biol Chem 271: 21037–21040

    Google Scholar 

  • Bielski BHJ, Richter HW (1977) A study of the superoxide radical chemistry by stopped-flow radiolysis and radiation-induced oxygen consumption. J Am Chem Soc 99: 3019–3323

    Google Scholar 

  • —, Cabelli DE, Arudi RL (1985) Reactivity of HO2/O2 radicals in aqueous solutions. J Phys Chem Ref Data 14: 1041–1062

    Google Scholar 

  • Carlioz A, Touati D (1986) Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J 5: 623–630

    Google Scholar 

  • Czapski G, Golgstein S, Meyerstein D (1988) What is unique about superoxide toxicity as compared to other biological reductants: a hypothesis. Free Radic Res Commun 4: 231–236

    Google Scholar 

  • Davies KJA, Lin WL (1988a) Degradation of oxidatively denatured proteins in Escherichia coli. Free Radic Biol Med 5: 215–223

    Google Scholar 

  • — — (1988b) Oxidatively denatured proteins are degraded by an ATP-independent proteolytic pathway in Escherichia coli. Free Radic Biol Med 5: 225–236

    Google Scholar 

  • DiGuiseppi J, Fridovich I (1984) The toxicology of molecular oxygen. Crit Rev Toxicol 12: 315–342

    Google Scholar 

  • Dukan S, Nystrom T (1999) Oxidative stress defense and deterioration of growth-arrestedEscherichia coli cells. J Biol Chem 274: 26027–26032

    Google Scholar 

  • Farr SB, D'Ari R, Touati D (1986) Oxygen-dependant mutagenesis in Escherichia coli lacking superoxide dismutase. Proc Natl Acad Sci USA 83: 8268–8272

    Google Scholar 

  • Fee JA (1982) Is superoxide important in oxygen poisoning? Trends Biochem Sci 7: 84–86

    Google Scholar 

  • Flint DH, Tuminello JF, Emptage NH (1993) The inactivation of Fe-S cluster containing hydrolyases by superoxide. J Biol Chem 268: 22369–22376

    Google Scholar 

  • Gardner P, Fridovich I (1991a) Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. J Biol Chem 266: 1478–1483

    Google Scholar 

  • — — (1991b) Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266: 19328–19333

    Google Scholar 

  • Halliwell B (1978) Superoxide-dependant formation of hydroxyl radicals in the presence of iron chelates: is it a mechanism for hydroxyl radical production in biological systems? FEBS Lett 92: 321–326

    Google Scholar 

  • Hausladen A, Fridovich I (1994) Superoxide and peroxynitrite inactivate aconitase, but nitric oxide does not. J Biol Chem 269: 29405–29408

    Google Scholar 

  • Keyer K, Imlay J (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93: 13635–13640

    Google Scholar 

  • Kuo CF, Mashino T, Fridovich I (1987) alpha,beta-Dihydroxyisovaleriate dehydratase: a superoxide-sensitive enzyme. J Biol Chem 262: 4724–4727

    Google Scholar 

  • Liochev S (1996) The role of iron-sulfur clusters in in vivo hydroxyl radical production. Free Radic Res 25: 369–384

    Google Scholar 

  • —, Fridovich I (1993) Modulation of the fumarases of Escherichia coli in response to oxidative stress. Arch Biochem Biophys 301: 379–384

    Google Scholar 

  • — — (1994) The role of O2 in the production of HO·: in vitro and in vivo. Free Radic Biol Med 16: 29–33

    Google Scholar 

  • Maringanti S, Imlay J (1999) An intracellular iron chelator pleiotropically suppresses enzymatic and growth defects of superoxide dismutase-deflcient Escherichia coli. J Bacteriol 181: 3792–3802

    Google Scholar 

  • McCord JM, Day ED (1978) Superoxide-dependant production of hydroxyl radical catalyzed by iron-EDTA complex. FEBS Lett 86: 139–142

    Google Scholar 

  • —, Fridovich I (1969) Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049–6055

    Google Scholar 

  • McCord JM, Keele BB, Fridovich I (1971) An enzyme based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc Natl Acad Sci USA 68: 1024–1027

    Google Scholar 

  • Sawyer DT, Valentine JS (1981) How super is superoxide? Accounts Chem Res 14: 393–400

    Google Scholar 

  • Stadtman ER, Oliver CN (1991) Metal-catalyzed oxidation of proteins. J Biol Chem 266: 2005–2008

    Google Scholar 

  • Winterbourn C (1981) Hydroxyl radical production in body fluids: roles of metal ions, ascorbate and superoxide. Biochem J 198: 125–131

    Google Scholar 

  • — (1993) Superoxide as an intracellular sink. Free Radic Biol Med 14: 85–90

    Google Scholar 

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Benov, L. How superoxide radical damages the cell. Protoplasma 217, 33–36 (2001). https://doi.org/10.1007/BF01289410

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