SUPEROXIDE RADICALS, SUPEROXIDE DISMUTASES AND THE AEROBIC LIFESTYLE

Abstract— The superoxide radical (O‐2) is a commonplace product of the biological reduction of molecular oxygen and plays an important role in oxygen toxicity. Superoxide dismutases (SOD) catalytically scavenge this radical and are the primary defense against its cytotoxicity. The data which support these statements have been briefly reviewed. Oxygen enhances the lethality of certain antibiotics, such as streptonigrin, and of ionizing radiation as well. The role of O‐2 in the enhancements is presented and the basis of the radioprotective effects of SOD discussed. Several more recent developments are presented in detail including: (a) The induction of the MnSOD of E. coli upon exposure to very low levels of oxygen, (b) The changes in SOD in E. coli as a function of nutritional state, during culture in a chemostat. (c) A convenient new assay and activity stain for SOD.

[1]  W. Ganong,et al.  Evidence for the Involvement of Superoxide Anion in Dopamine-β-Hydroxylase System 1 , 1974, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.

[2]  K. Puget,et al.  Isolation of a new copper-containing superoxide dismutase bacteriocuprein. , 1974, Biochemical and biophysical research communications.

[3]  I. Fridovich,et al.  An iron-containing superoxide dismutase from Escherichia coli. , 1973, The Journal of biological chemistry.

[4]  B. Babior,et al.  Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. , 1973, The Journal of clinical investigation.

[5]  I. Fridovich,et al.  An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[6]  Fritz Haber,et al.  The catalytic decomposition of hydrogen peroxide by iron salts , 1934 .

[7]  I. Fridovich,et al.  Physiological function of superoxide dismutase in glucose-limited chemostat cultures of Escherichia coli , 1977, Journal of bacteriology.

[8]  B. Halliwell.  SUPEROXIDE DISMUTASE, CATALASE AND GLUTATHIONE PEROXIDASE: SOLUTIONS TO THE PROBLEMS OF LIVING WITH OXYGEN , 1974 .

[9]  A. Petkau,et al.  Radioprotection of mice by superoxide dismutase. , 1975, Biochemical and biophysical research communications.

[10]  I. Fridovich,et al.  Superoxide Dismutases of Escherichia coli: Intracellular Localization and Functions , 1973, Journal of bacteriology.

[11]  J. McCord,et al.  Superoxide dismutases in polymorphonuclear leukocytes. , 1974, The Journal of clinical investigation.

[12]  F. Hirata,et al.  Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes. , 1977, The Journal of biological chemistry.

[13]  I. Fridovich,et al.  A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase. , 1970, The Journal of biological chemistry.

[14]  I. Fridovich,et al.  Superoxide Dismutase and the Oxygen Effect , 1973 .

[15]  K. Asada,et al.  A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii. Enzymologic and spectrophotometric properties. , 1976, The Journal of biological chemistry.

[16]  Ōyanagui Yoshihiko.  Participation of superoxide anions at the prostaglandin phase of carrageenan foot-oedema , 1976 .

[17]  I. Fridovich,et al.  The reduction of cytochrome c by milk xanthine oxidase. , 1968, The Journal of biological chemistry.

[18]  I. Fridovich,et al.  Intracellular localization of the superoxide dismutases of Escherichia coli: a reevaluation , 1977, Journal of bacteriology.

[19]  B. Halliwell.  Hydroxylation of p-Coumaric acid by illuminated chloroplasts. The role of superoxide. , 1975, European journal of biochemistry.

[20]  I. Fridovich,et al.  Oxygen Toxicity and the Superoxide Dismutase , 1973, Journal of bacteriology.

[21]  M. Buckingham,et al.  Effects of superoxide radicals on myoblast growth and differentiation. , 1974, Biochemical and biophysical research communications.

[22]  A. Petkau,et al.  Letter: Protection of post-irradiated mice by superoxide dismutase. , 1976, International journal of radiation biology and related studies in physics, chemistry, and medicine.

[23]  L. Oberley,et al.  Superoxide lon as the cause of the oxygen effect. , 1976, Radiation research.

[24]  J. Harris,et al.  Evolutionary relationships in superoxide dismutase , 1975, FEBS letters.

[25]  I. Fridovich.  Superoxide Radical and Superoxide Dismutase , 1972 .

[26]  J. V. van Hemmen,et al.  Inactivation of biologically active DNA by gamma-ray-induced superoxide radicals and their dismutation products singlet molecular oxygen and hydrogen peroxide. , 1975, Biochimica et biophysica acta.

[27]  R. Hill,et al.  Sequence homologies among bacterial and mitochondrial superoxide dismutases. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[28]  I. Fridovich,et al.  Superoxide dismutase: a photochemical augmentation assay. , 1977, Archives of biochemistry and biophysics.

[29]  E. W. Kellogg,et al.  Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system. , 1975, The Journal of biological chemistry.

[30]  F. Hirata,et al.  Studies on indoleamine 2,3-dioxygenase. I. Superoxide anion as substrate. , 1975, The Journal of biological chemistry.

[31]  J. McCord,et al.  Free radicals and inflammation. Protection of phagocytosine leukocytes by superoxide dismutase. , 1975, The Journal of clinical investigation.

[32]  I. Fridovich,et al.  Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. , 1971, Analytical biochemistry.

[33]  I. Fridovich.  Superoxide dismutases: studies of structure and mechanism. , 1976, Advances in experimental medicine and biology.

[34]  I. Fridovich,et al.  Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. , 1970, The Journal of biological chemistry.

[35]  I. Fridovich,et al.  Superoxide dismutase and the oxygen enhancement of radiation lethality. , 1976, Archives of biochemistry and biophysics.

[36]  B. Babior,et al.  Biological defense mechanisms. Evidence for the participation of superoxide in bacterial killing by xanthine oxidase. , 1975, The Journal of laboratory and clinical medicine.

[37]  I. Fridovich,et al.  Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli , 1977, Journal of bacteriology.

[38]  I. Fridovich,et al.  Superoxide dismutase and peroxidase: a positive activity stain applicable to polyacrylamide gel electropherograms. , 1977, Archives of biochemistry and biophysics.

[39]  I. Fridovich,et al.  Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). , 1969, The Journal of biological chemistry.