The Toxicology of Molecular Oxygen

References

• Kaye D. Effect of hyperbaric oxygen on aerobic bacteria. in vitro and in vivo, Proc. Soc. Exp. Biol. Med. 1967; 124: 1090
   PubMed Web of Science ®Google Scholar
• Gregory E. M., Goscin S. A., Fridovich I. Superoxide dismutase and oxygen toxicity in a eukaryote. J. Bacteriol. 1974; 117: 456
   PubMed Web of Science ®Google Scholar
• Pulich W. M., Jr. Resistance to high oxygen tension, streptonigrin, and ultraviolet irradiation in the green alga. Chlorella sorokiniana strain ORS, J. Cell Biol. 1974; 62: 904
   PubMed Web of Science ®Google Scholar
• Fenn W. O., Gerschman R., Gilbert D. L., Terwilliger D. E., Cothran F. V. Mutagenic effects of high oxygen tensions on. Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 1957; 43: 1027
   PubMed Web of Science ®Google Scholar
• Bruyninckx W. J., Mason H. S., Morse S. A. Are physiological oxygen concentrations mutagenic. Nature (London) 1978; 274: 606
   PubMed Web of Science ®Google Scholar
• Soloway A. H., LeQuesne P. W. Potential endogenous mutagens/carcinogens. J. Theor. Biol. 1980; 85: 153
   PubMed Web of Science ®Google Scholar
• Harley J. B., Flaks J. G., Goldfine H., Bayer M. E., Rasmussen H. Hyperbaric oxygen toxicity and ribosome destruction inEscherichia coli K12. Can. J. Microbiol. 1981; 27: 44
   PubMed Web of Science ®Google Scholar
• Elstner E. F. Oxygen activation and oxygen toxicity. Ann. Rev. Plant Physiol. 1982; 33: 73
   Google Scholar
• Rabinowitch H., Fridovich I. Superoxide radicals, superoxide dismutases and oxygen toxicity in plants. Photochem. Photobiol. 1983; 37: 679
   Web of Science ®Google Scholar
• Perrins D. J. D., Davis J. C. Enhancement of healing in soft tissue wounds. Hyperbaric Oxygen Therapy, J. E. Davis, T. K. Hunt. Undersea Medical Society, , Maryland 1977; 229
   Google Scholar
• Silver I. A. Oxygen tension in the clinical situation. Oxygen and Living Processes, D. L. Gilbert. Springer-Verlag, New York 1981; 358
   Google Scholar
• Huber G. L., Drath D. P. Pulmonary oxygen toxicity. Oxygen and Living Processes, D. L. Gilbert. Springer-Verlag, New York 1981; 273
   Google Scholar
• Terry T.-L. Extreme prematurity and fibroblastic overgrowth of persistent vascular sheath behind each crystalline lens. Am. J. Ophthalmol. 1942; 25: 203
   Google Scholar
• Patz A. Retrolental fibroplasia. Survey Ophthalmol. 1969; 14: 1
   PubMedGoogle Scholar
• Ngai S. H., Levy A., Finck A. D., Yang J. C., Spector S. Central nervous system toxicity of hyperbaric oxygen—effects of light, norepinephrine depletion and beta-adrenergic blockade. Neuropharm. 1977; 16: 675
   PubMed Web of Science ®Google Scholar
• Balentine J. D. Experimental pathology of oxygen toxicity. Oxygen and Physiological Function, F. F. Jobsis. Professional Information Library, Dallas, Tex. 1978; 331
   Google Scholar
• Kovachich G. B., Haugaard N. Biochemical aspects of oxygen toxicity in the metazoa. Oxygen and Living Processes, D. L. Gilbert. Springer-Verlag, New York 1981; 210
   Google Scholar
• Bean I. W., Johnson P. C. Epinephrine and neurogenic factors in pulmonary edema and CNS reactions induced by oxygen at high pressure. Am. J. Physiol. 1955; 180: 438
   PubMedGoogle Scholar
• Taylor D. W. Effects of high oxygen pressures on adrenalectomized, treated and untreated rats. J. Physiol. 1954; 125: 46P
   PubMed Web of Science ®Google Scholar
• Mitchell J. S. Some clinical and laboratory studies of chemical radiosensitizers. Acta Unio. Int. Cancer 1957; 13: 450
   PubMedGoogle Scholar
• Misra H. P., Fridovich I. Superoxide dismutase and the oxygen enhancement of radiation lethality. Arch. Biochem. Biophys. 1976; 176: 577
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Paraquat andEscherichia coli. Mechanism of production of extracellular superoxide radical. J. Biol. Chem. 1979; 254: 10846
   PubMed Web of Science ®Google Scholar
• Oshida R., Takehashi T. Increased DNA chain breakage by combined action of bleomycin and superoxide radical. Biochem. Biophys. Res. Commun. 1975; 66: 1432
   PubMed Web of Science ®Google Scholar
• Onishi T., Iwata H., Takagi K. Effects of reducing and oxidizing agents on the action of bleomycin. J. Biochem. (Tokyo) 1975; 77: 745
   PubMed Web of Science ®Google Scholar
• Sausville E. A., Peisach P., Horwitz S. A role for ferrous ion and oxygen in the degradation of DNA by bleomycin. Biochem. Biophys. Res. Commun. 1976; 73: 814
   PubMed Web of Science ®Google Scholar
• Winterbourn C. C. Evidence for the production of hydroxyl radicals from the adriamycin semiquinone and H2O2. FEBS Lett. 1981; 136: 89
   Web of Science ®Google Scholar
• Buettner G. R., Oberley L. W. The production of hydroxyl radical by tallysomycin and copper(II). FEBS Lett. 1979; 101: 333
   PubMed Web of Science ®Google Scholar
• Boveris A., Docampo R., Turrens J. F., Stoppani A. O. M. Effect of β-lapachone on superoxide anion and hydrogen peroxide production in. Trypanosoma cruzi, Biochem. J. 1978; 175: 431
   Google Scholar
• White H. L., White J. R. Lethal action and metabolic effects of streptonigrin on, Escherichia coli. Mol. Pharm. 1968; 4: 549
   Web of Science ®Google Scholar
• Lown J. W., Joshua A. V., Lee J. S. Molecular mechanisms of binding and single-strand scission of deoxyribonucleic acid by the antitumor antibiotics Saframycins A and C. Biochemistry 1982; 21: 419
   PubMed Web of Science ®Google Scholar
• Bonikos D. S., Bensch K. G., Northway W. H., Jr. Oxygen toxicity in the newborn. The effect of chronic continuous 100 percent oxygen exposure on the lungs of newborn mice. Am. J. Pathol. 1976; 85: 623
   PubMed Web of Science ®Google Scholar
• Baeyens D. A., Hoffert J. R., Fromm P. O. A comparative study of oxygen toxicity in the retina, brain and liver of the teleost, amphibian and mammal. Comp. Biochem. Physiol. 1973; 45A: 925
   Google Scholar
• Tierney D. F., Ayers L., Kasuyama R. S. Altered sensitivity to oxygen toxicity. Am. Rev. Resp. Dis. 1977; 115: 59, Suppl.
   PubMed Web of Science ®Google Scholar
• Munkres K. D. Ageing ofNeurospora crassa. VIII. Lethality and mutagenicity of ferrous ions, ascorbic acid, and malondialdehyde. Mech. Ageing Dev. 1979; 10: 249
   PubMed Web of Science ®Google Scholar
• Kehrer H. P., Autor A. P. The effect of dietary fatty acids on the composition of adult rat lung lipids: relationship to oxygen toxicity. Toxicol. Appl. Pharmacol. 1978; 44: 423
   PubMed Web of Science ®Google Scholar
• Morris J. G. Oxygen and the obligate anaerobe. J. Appl. Bacteriol. 1976; 40: 229
   PubMedGoogle Scholar
• Drozd J., Postgate J. R. Effects of oxygen on acetylene reduction, cytochrome content and respiratory activity of. Azotobacter chroococcum, J. Gen. Microbiol. 1970; 63: 63
   PubMedGoogle Scholar
• Stadie W. C., Haugaard N. Oxygen poisoning. V. J. Biol. Chem. 1945; 161: 153
   PubMedGoogle Scholar
• Stadie W. C., Haugaard N. Oxygen poisoning. VII. J. Biol. Chem. 1945; 161: 175
   PubMedGoogle Scholar
• Wood J. D., Watson W. J., Stacey N. E. A comparative study of hyperbaric oxygen-induced and drug-induced convulsions with particular reference to γ-aminobutyric acid metabolism. J. Neurochem. 1966; 13: 361
   Web of Science ®Google Scholar
• Alderman J. L., Culver B. W., Shellenberger M. K. An examination of the role of γ-aminobutyric acid (Gaba) in hyperbaric oxygen-induced convulsions in the rat. I. Effects of increased γ-aminobutyric acid and protective agents. J. Pharmacol. Exp. Ther. 1974; 190: 334
   PubMed Web of Science ®Google Scholar
• Arias I. M., Jakoby W. B. Glutathione: Metabolism and Function. Raven Press, New York 1976
   Google Scholar
• Brown O. R., Yein F. Sensitivity to and site of oxygen poisoning in. Escherichia coli, Am. J. Clin. Nutr. 1979; 32: 267
   Web of Science ®Google Scholar
• Chance B., Sies H., Boveris A. Hydrogen peroxide metabolism in mammalian organs. Physiol. Rev. 1979; 59: 527
   PubMed Web of Science ®Google Scholar
• Hildebrandt A. G., Roots I. Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Arch. Biochem. Biophys. 1975; 171: 385
   PubMed Web of Science ®Google Scholar
• Nohl H., Hegner D. Do mitochondria produce oxygen radicals in vivo. Eur. J. Biochem. 1978; 82: 563
   PubMedGoogle Scholar
• Asada K., Takahashi M., Tanaka K., Nakano Y. Formation of active oxygen and its fate in chloroplasts. Biochemical and Medical Aspects of Active Oxygen, O. Hayaishi, K. Asada. University of Tokyo Press, Tokyo 1977; 45
   Google Scholar
• Weiss S. J., Young J., LoBuglio A. F., Slivka A., Nimeh N. F. Role of hydrogen peroxide in neutrophil-mediated destruction of cultured endothelial cells. J. Clin. Invest. 1981; 68: 714
   PubMed Web of Science ®Google Scholar
• Holmberg K., Hallender H. O. Production of bactericidal concentrations of hydrogen peroxide by. Streptococcus sanguis, Arch. Oral. Biol. 1973; 18: 423
   PubMed Web of Science ®Google Scholar
• Malke H., Starke R., Jacob H. E., Kohler W. Bacteriocine-like activity of group-A streptococci due to the production of peroxide. J. Med. Microbiol. 1974; 7: 367
   PubMed Web of Science ®Google Scholar
• Oshino N., Jaieson D., Sugano T., Chance B. Optical measurement of the catalase-hydrogen peroxide intermediate (Compound I) in the liver of anaesthetized rats and its implication to hydrogen peroxide production. in situ, Biochem. J. 1975; 146: 67
   PubMed Web of Science ®Google Scholar
• Walling C. Fenton's reagent revisited. Acc. Chem. Res. 1975; 8: 125
   Web of Science ®Google Scholar
• Gifford G. D. Toxicity of hyperbaric oxygen to bacteria in relation to the cell cycle and catalase synthesis. J. Gen. Microbiol. 1968; 52: 375
   Google Scholar
• Gerschman R., Gilbert D. L., Nye S. W., Dwyer P., Fenn W. O. Oxygen poisoning and X-irradiation: a mechanism in common. Science 1954; 119: 623
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. The reduction of cytochromec by milk xanthine oxidase. J. Biol. Chem. 1968; 243: 5753
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 1969; 244: 6049
   PubMed Web of Science ®Google Scholar
• Antonini E., Brunori M., Greenwood C., Malmstrom B. G. Catalytic mechanism of cytochrome oxidase. Nature (London) 1970; 228: 936
   PubMed Web of Science ®Google Scholar
• Taube H. Mechanisms of oxidation with oxygen. J. Gen. Physiol. 1965; 49: 29, (Suppl.)
   PubMed Web of Science ®Google Scholar
• Misra H. P., Fridovich I. The univalent reduction of oxygen by reduced flavins and quinones. J. Biol. Chem. 1972; 247: 188
   PubMed Web of Science ®Google Scholar
• Ballou D., Palmer G., Massey V. Direct demonstration of superoxide anion production during the oxidation of reduced flavin and of its catalytic decomposition by erythrocuprein. Biochem. Biophys. Res. Commun. 1969; 36: 898
   PubMed Web of Science ®Google Scholar
• Misra H. P., Fridovich I. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J. Biol. Chem. 1972; 247: 3170
   PubMed Web of Science ®Google Scholar
• Cohen G., Heikkila R. E. The generation of hydrogen peroxide, superoxide radical, and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents. J. Biol. Chem. 1974; 249: 2447
   PubMed Web of Science ®Google Scholar
• Misra H. P. Generation of superoxide free radical during the autoxidation of thiols. J. Biol. Chem. 1974; 249: 2151
   PubMed Web of Science ®Google Scholar
• Al-Thannon A. A., Barton J. P., Packer J. E., Sims R. J., Trumbore C. N., Winchester R. V. The radiolysis of aqueous solutions of cysteine in the presence of oxygen. Int. J. Radiat. Phys. Chem. 1974; 6: 233
   Google Scholar
• Lal M. 60 Co-gamma radiolysis of cysteine in aerated solutions at pH 5.5 to 6.0. Rad. Effects 1974; 22: 237
   Google Scholar
• Baccanari D. P. Coupled oxidation of NADPH with thiols at neutral pH. Arch. Biochem. Biophys. 1978; 191: 351
   PubMed Web of Science ®Google Scholar
• Fisher D. B., Kaufman S. Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase. J. Biol. Chem. 1973; 248: 4300
   PubMed Web of Science ®Google Scholar
• Heikkila R. E., Cohen G. The generation of the superoxide radical by 2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropterin (DMPH4). Experientia 1975; 31: 169
   Google Scholar
• Nishikimi M. The generation of superoxide anion in the reaction of tetrahydropteridines with molecular oxygen. Arch. Biochem. Biophys. 1975; 166: 273
   PubMed Web of Science ®Google Scholar
• Hasegawa H., Nakanishi N., Akino M. Stoichiometric studies on the oxidation of tetrahydropterin with ferric-cytochromec. J. Biochem. 1978; 84: 499
   PubMed Web of Science ®Google Scholar
• Orme-Johnson W. H., Beinert H. On the formation of the superoxide anion radical during the reaction of reduced iron-sulfur proteins with oxygen. Biochem. Biophys. Res. Commun. 1969; 36: 905
   PubMed Web of Science ®Google Scholar
• Nilsson R., Pick F. M., Bray R. C. EPR studies on reduction of oxygen to superoxide by some biochemical systems. Biochim. Biophys. Acta 1969; 192: 145
   PubMedGoogle Scholar
• Misra H. P., Fridovich I. The generation of superoxide radical during the autoxidation of ferredoxins. J. Biol. Chem. 1971; 246: 6086
   Web of Science ®Google Scholar
• Nakamura S., Kimura T. Studies on aggregated multienzyme systems. Stimulation of oxygen uptake of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase-ferredoxin complex by cytochrome. c, J. Biol. Chem. 1972; 247: 6462
   PubMed Web of Science ®Google Scholar
• Allen J. F. A two-step mechanism for the photosynthetic reduction of oxygen by ferredoxin. Biochem. Biophys. Res. Commun. 1975; 66: 36
   PubMed Web of Science ®Google Scholar
• Marklund S., 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
   PubMedGoogle Scholar
• Cassell R. H., Fridovich I. The role of superoxide radical in the autoxidation of cytochrome. c, Biochemistry. 1975; 14: 1866
   PubMed Web of Science ®Google Scholar
• Berman M. C., Adnams C. M., Ivanetich K. M., Kench J. E. Autoxidation of soluble trypsincleaved microsomal ferrocytochrome b5 and formation of superoxide radicals. Biochem. J. 1976; 157: 237
   PubMed Web of Science ®Google Scholar
• Gotoh T., Shikama K. Generation of the superoxide radical during autoxidation of oxymyoglobin. J. Biochem. 1976; 80: 397
   PubMed Web of Science ®Google Scholar
• Auclair C., DeProst D., Hakim J. Superoxide anion production by liver microsomes from phenobarbital treated rats. Biochem. Pharm. 1978; 27: 355
   PubMed Web of Science ®Google Scholar
• Felix C. C., Hyde J. S., Sarna T., Sealy R. C. Melanin photoreactions in aerated media: electron spin resonance evidence for production of superoxide and hydrogen peroxide. Biochem. Biophys. Res. Commun. 1978; 84: 335
   PubMed Web of Science ®Google Scholar
• Buettner G. R., Oberley L. W. The apparent production of superoxide and hydroxyl radicals by hematoporphyrin and light as seen by spin-trapping. FEBS Lett. 1980; 121: 161
   PubMed Web of Science ®Google Scholar
• Inoue K., Matsuura T., Saito I. Photogeneration of superoxide ion and hydrogen peroxide from tryptophan and its photooxidation products: the role of 3-α-hydroperoxypyrrolidinoindole. Photochem. Photobiol. 1982; 35: 133
   Web of Science ®Google Scholar
• Carrell R. W., Krisnamoorthy R., Winterbourne C. C. Haemoglobin autoxidation. The risk to the red cell and the contribution of copper. The Red Cell, G. J. Brewer. Alan R. Liss, New York 1979; 687
   Google Scholar
• Rajagopalan K. V., Fridovich I., Handler P. Aldehyde oxidase. I. J. Biol. Chem. 1962; 237: 922
   PubMed Web of Science ®Google Scholar
• Badwey J. A., Robinson J. M., Karnovsky M. J., Karnovsky M. L. Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. J. Biol. Chem. 1981; 256: 3479
   PubMed Web of Science ®Google Scholar
• Forman H. J., Kennedy J. Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid. J. Biol. Chem. 1975; 250: 4322
   PubMed Web of Science ®Google Scholar
• Miller R. W. A high molecular weight dihydro-orotate dehydrogenase ofNeurospora crassa. Purification and properties of the enzyme. Can. J. Biochem. 1975; 53: 1288
   PubMedGoogle Scholar
• Taniguchi T., Hirata F., Hayaishi O. Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes. J. Biol. Chem. 1977; 252: 2774
   PubMed Web of Science ®Google Scholar
• Hirata F., Ohnishi T., Hayaishi O. Indoleamine 2,3-dioxygenase. J. Biol. Chem. 1977; 252: 4637
   PubMed Web of Science ®Google Scholar
• Kido T., Soda K. A new oxygenase, 2-nitropropane dioxygenase ofHansenula mrakii. Enzymologic and spectrophotometric properties. J. Biol. Chem. 1976; 251: 6994
   PubMed Web of Science ®Google Scholar
• Kido T., Hashizume K., Soda K., Asada K. Generation and participation of O2-in 2-nitropropane dioxygenase reaction. Photochem. Photobiol. 1978; 28: 729
   Web of Science ®Google Scholar
• Turrens J. F., Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 1980; 191: 421
   PubMed Web of Science ®Google Scholar
• Bosterling B., Trudell J. R. Spin trap evidence for production of superoxide radical anions by purified NADPH-cytochrome P-450 reductase. Biochem. Biophys. Res. Commun. 1981; 98: 569
   PubMed Web of Science ®Google Scholar
• Ingelman-Sundberg M., Johansson I. The mechanism of cytochrome P-450-dependent oxidation of ethanol in reconstituted membrane vesicles. J. Biol. Chem. 1981; 256: 6321
   PubMed Web of Science ®Google Scholar
• Loschen G., Azzi A., Richter C., Flohe L. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett. 1974; 42: 68
   PubMed Web of Science ®Google Scholar
• Boveris A., Cadenas E. Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration. FEBS Lett. 1975; 54: 311
   PubMed Web of Science ®Google Scholar
• Azzi A., Montecucco C., Richter C. The use of acetylated ferricytochromec for the detection of superoxide radicals produced in biological membranes. Biochem. Biophys. Res. Commun. 1975; 65: 597
   PubMed Web of Science ®Google Scholar
• Tyler D. D. A protective function of superoxide dismutase during respiratory chain activity. Biochim. Biophys. Acta 1975; 396: 335
   PubMedGoogle Scholar
• Boveris A., Cadenas E., Stoppani A. O. M. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 1976; 156: 435
   PubMed Web of Science ®Google Scholar
• Cadenas E., Boveris A., Ragan C. I., Stoppani A. O. M. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochromec reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 1977; 180: 248
   PubMed Web of Science ®Google Scholar
• Boveris A. Mitochondrial production of superoxide radical and hydrogen peroxide. Adv. Exp. Med. Biol. 1977; 78: 67
   PubMedGoogle Scholar
• Huq S., Palmer J. M. Superoxide and hydrogen peroxide production in cyanide-resistantArum maculatum mitochondria. Plant Sci. Lett. 1978; 11: 351
   Google Scholar
• Rich P. R., Bonner W. D., Jr. The sites of superoxide anion generation in higher plant mitochondria. Arch. Biochem. Biophys. 1978; 188: 206
   PubMed Web of Science ®Google Scholar
• Boveris A., Sanchez R. A., Beconi M. T. Antimycin- and cyanide-resistant respiration and superoxide anion production in fresh and aged potato tuber mitochondria. FEBS Lett. 1978; 92: 333
   Web of Science ®Google Scholar
• Turrens J. F., Freeman B. A., Levitt J. G., Crapo J. D. The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch. Biochem. Biophys. 1982; 217: 401
   PubMed Web of Science ®Google Scholar
• Patton S. E., Rosen G. M., Rauckman E. J. Superoxide production by purified hamster hepatic nuclei. Mol. Pharm. 1980; 18: 588
   PubMed Web of Science ®Google Scholar
• Epel B. L., Neumann J. The mechanism of the oxidation of ascorbate and Mn2+ by choloroplasts. The role of the radical superoxide. Biochim. Biophys. Acta 1973; 325: 520
   PubMedGoogle Scholar
• Asada K., Kiso K., Yoshikawa K. Univalent reduction of molecular oxygen spinach by chloroplasts on illumination. J. Biol. Chem. 1974; 249: 2175
   PubMed Web of Science ®Google Scholar
• Allen J. F., Hall D. O. The relationship of oxygen uptake to electron transport in photosystem I of isolated chloroplasts: the role of superoxide and ascorbate. Biochem. Biophys. Res. Commun. 1974; 58: 579
   PubMed Web of Science ®Google Scholar
• Harbour J. R., Bolton J. R. Superoxide formation in spinach chloroplasts: electron spin resonance detection by spin trapping. Biochem. Biophys. Res. Commun. 1975; 64: 803
   PubMed Web of Science ®Google Scholar
• Halliwell B. The chloroplast at work. A review of recent developments in our understanding of chloroplast metabolism. Prog. Biophys. Molec. Biol. 1978; 33: 1
   PubMed Web of Science ®Google Scholar
• Montgomery M. R. Paraquat toxicity and pulmonary superoxide dismutase: an enzymic deficiency of lung microsomes. Res. Commun. Chem. Pathol. Pharmacol. 1977; 16: 155
   PubMedGoogle Scholar
• Richter C., Azzi A., Weser U., Wendel A. Hepatic microsomal dealkylations. J. Biol. Chem. 1977; 252: 5061
   PubMedGoogle Scholar
• Kuthan H., Tsuji H., Graf H., Ullrich V. Generation of superoxide anion as a source of hydrogen peroxide in a reconstituted monooxygenase system. FEBS Lett. 1978; 91: 343
   PubMed Web of Science ®Google Scholar
• Talcott R. E., Shu H., Wei E. T. Dissociation of microsomal oxygen reduction and lipid peroxidation with the electron acceptors, paraquat and menadione. Biochem. Pharmacol. 1979; 28: 665
   PubMed Web of Science ®Google Scholar
• Sasame H. A., Boyd M. R. Superoxide and hydrogen peroxide production and NADPH oxidation stimulated by nitrofurantoin in lung microsomes: possible implications for toxicity. Life Sci. 1979; 24: 1091
   PubMed Web of Science ®Google Scholar
• Kuthan H., Ullrich V., Estabrook R. W. A quantitative test for superoxide radicals produced in biological systems. Biochem. J. 1982; 203: 551
   PubMed Web of Science ®Google Scholar
• Babior B. M., Kipnes R. S., Curnutte J. T. Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest. 1973; 52: 741
   PubMed Web of Science ®Google Scholar
• Stokes S. H., Davis W. B., Sorber W. A. Effect of phagocytosis on superoxide anion production and superoxide dismutase levels in BCG-activated and normal rabbit alveolar macrophages. J. Reticuloendothel. Soc. 1978; 24: 101
   PubMedGoogle Scholar
• Markert M., Allaz M.-J., Frei J. Continuous monitoring of oxygen consumption and superoxide production by particle-stimulated human polymorphonuclear leukocytes. FEBS Lett. 1980; 113: 225
   PubMed Web of Science ®Google Scholar
• Nakagawara A., Nathan C. F., Cohn Z. A. Hydrogen peroxide metabolism in human monocytes during differentiation. in vitro, J. Clin. Invest. 1981; 68: 1243
   PubMed Web of Science ®Google Scholar
• Hoffman M., Autor A. P. Production of superoxide anion by an NADPH-oxidase from rat pulmonary macrophages. FEBS Lett. 1980; 121: 352
   PubMed Web of Science ®Google Scholar
• Simchowitz L., Atkinson J. P., Spilberg I. Stimulus-specific deactivation of chemotactic factorinduced cyclic AMP response and superoxide generation by human neutrophils. J. Clin. Invest. 1980; 66: 736
   PubMed Web of Science ®Google Scholar
• Babior B. M., Peters W. A. The O2-producing enzyme of human neutrophils. Further properties. J. Biol. Chem. 1981; 256: 2321
   PubMed Web of Science ®Google Scholar
• Light D. R., Walsh C., O'Callaghan A. M., Goetzl E. J., Tauber A. I. Characteristics of the cofactor requirements for the superoxide-generating NADPH oxidase of human polymorphonuclear leukocytes. Biochemistry 1981; 20: 1468
   PubMed Web of Science ®Google Scholar
• Babior G. L., Rosin R. E., McMurrich B. J., Peters W. A., Babior B. M. Arrangement of the respiratory burst oxidase in the plasma membrane of the neutrophil. J. Clin. Invest. 1981; 67: 1724
   PubMed Web of Science ®Google Scholar
• Andrew P. W., Lowrie D. B., Jackett P. S., Peters T. J. Analytical subcellular fractionation of rabbit alveolar macrophages with particular reference to the subcellular localisation of pyridine nucleotide dependent superoxide-generating systems and superoxide dismutase. Biochim. Biophys. Acta 1980; 611: 61
   PubMedGoogle Scholar
• Curnutte J. T., Whitten D. M., Babior B. M. Defective superoxide production by granulocytes from patients with chronic granulomatous disease. N. Engl. J. Med. 1974; 290: 593
   PubMed Web of Science ®Google Scholar
• Babior B. M. Oxygen dependent microbial killing by phagocytes. N. Engl. J. Med. 1978; 298: 659, 298, 721, 1978
   PubMed Web of Science ®Google Scholar
• Britton L., Malinowski D. P., Fridovich I. Superoxide dismutase and oxygen metabolism inStreptococcus faecalis and comparisons with other organisms. J. Bacteriol. 1978; 134: 229
   PubMed Web of Science ®Google Scholar
• Bielski B. H. J., Allen A. O. Mechanism of the disproportionation of superoxide radicals. J. Phys. Chem. 1977; 81: 1048
   Web of Science ®Google Scholar
• Takahashi M., Asada K. A flash-photometric method for determination of reactivity of superoxide: application to superoxide dismutase assay. J. Biochem. 1982; 91: 889
   PubMed Web of Science ®Google Scholar
• Klug-Roth D., Fridovich I., Rabani J. Pulse radiolytic investigations of superoxide catalysed disproportionation. Mechanism for bovine superoxide dismutase. J. Am. Chem. Soc. 1973; 95: 2786
   PubMed Web of Science ®Google Scholar
• Pick M., Rabani J., Yost F., Fridovich I. The catalytic mechanism of the manganese-containing superoxide dismutase ofEscherichia coli studied by pulse radiolysis. J. Am. Chem. Soc. 1974; 96: 7329
   PubMed Web of Science ®Google Scholar
• Lavelle F., McAdam M. E., Fielden E. M., Roberts P. B. A pulse-radiolysis study of the catalytic mechanism of the iron-containing superoxide dismutase from. Photobacterium leiognathi, Biochem. J. 1977; 161: 3
   Google Scholar
• Koppenol W. H. The physiological role of the charge distribution of superoxide dismutase. Oxygen and Oxy-Radicals in Chemistry and Biology, M. A. J. Rodgers, E. L. Powers. Academic Press, New York 1981; 671
   Google Scholar
• Malinowski D. P., Fridovich I. Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. Biochemistry 1979; 18: 5909
   PubMed Web of Science ®Google Scholar
• Cudd A., Fridovich I. Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase. J. Biol. Chem. 1982; 257: 11443
   PubMed Web of Science ®Google Scholar
• Steinman H. M., Naik V. R., Abernethy J. L., Hill R. L. Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. J. Biol. Chem. 1974; 249: 7326
   PubMed Web of Science ®Google Scholar
• Forman H. J., Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J. Biol Chem. 1973; 248: 2645
   PubMed Web of Science ®Google Scholar
• Goscin S. A., Fridovich I. The purification and properties of superoxide dismutase from. Saccharomyces cerevisiae, Biochim. Biophys. Acta 1972; 289: 276
   PubMed Web of Science ®Google Scholar
• Misra H. P., Fridovich I. The purification and properties of superoxide dismutase from. Neurospora crassa, J. Biol. Chem. 1972; 247: 3410
   PubMed Web of Science ®Google Scholar
• Asada K., Urano M., Takahashi M. Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxide dismutase. Eur. J. Biochem. 1973; 36: 257
   PubMedGoogle Scholar
• Beauchamp C. O., Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochim. Biophys. Acta 1973; 317: 50
   PubMed Web of Science ®Google Scholar
• Weisiger R. A., Fridovich I. Superoxide dismutase. Organelle specificity. J. Biol. Chem. 1973; 248: 3582
   PubMed Web of Science ®Google Scholar
• Bannister J. V., Anastasi A., Bannister W. H. Cytosol superoxide-dismutase from swordfish (Xiphico-gladius L.) liver. Comp. Biochem. Physiol. 1977; 56B: 235
   Google Scholar
• Puget K., Michelson A. M. Isolation of a new copper-containing superoxide dismutase bacteriocuprein. Biochem. Biophys. Res. Commun. 1974; 58: 830
   PubMed Web of Science ®Google Scholar
• Steinman H. M. Copper-zinc superoxide dismutase fromCaulobacter crescentus CBI5. A novel bacteriocuprein form of the enzyme. J. Biol. Chem. 1982; 257: 10283
   PubMed Web of Science ®Google Scholar
• Martin J. P., Jr., Fridovich I. Evidence for a natural gene transfer from the ponyfish to its bioluminescent bacterial symbiont. Photobacter leiognathi, J. Biol. Chem. 1981; 256: 6080
   PubMed Web of Science ®Google Scholar
• Frants R. Occurrence of two superoxide dismutase systems in bovine tissues. Acta Acad. Abo. Ser. B 1973; 33: 17
   Google Scholar
• McCord J. M., Boyle J. A., Day E. D., Jr., Rizzolo L. L., Salin M. L. A manganese-containing superoxide dismutase from human liver. Superoxide and Superoxide Dismutases, M. A. Michelson, J. M. McCord, I. Fridovich. Academic Press, London 1977; 129
   Google Scholar
• Marklund S. Purification and characterization of a manganese containing superoxide dismutase from bovine heart mitochondria. Int. J. Biochem. 1978; 9: 299
   PubMedGoogle Scholar
• Sevilla F., Lopez-Gorge J., Del Rio L. A. Preliminary characterization of a Mn-containing superoxide dismutase from a higher plant (Pisum sativum L.). Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase, J. V. Bannister, H. A. O. Hill. Elsevier/North-Holland, New York 1980; 185
   Google Scholar
• Baum J. A., Scandalios J. G. Isolation and characterization of the cytosolic and mitochondrial superoxide dismutases of maize. Arch. Biochem. Biophys. 1981; 206: 249
   PubMed Web of Science ®Google Scholar
• Steinman H. M., Hill R. L. Sequence homologies among bacterial and mitochondrial superoxide dismutases. Proc. Natl. Acad. Sci. U.S.A. 1973; 70: 3725
   PubMed Web of Science ®Google Scholar
• Uzzell T., Spolsky C. Mitochondria and plastids as endosymbionts: a revival of special creation. Am. Sci. 1974; 62: 334
   PubMed Web of Science ®Google Scholar
• Chikata Y., Kusunose E., Ichihara K. Purification of superoxide dismutases from. Mycobacterium phlei, Osaka City Med. J. 1975; 21: 127
   PubMedGoogle Scholar
• Sato S., Harris J. I. Superoxide dismutase fromThermus aquaticus. Isolation and characterization of manganese and apo enzymes. Eur. J. Biochem. 1977; 73: 373
   PubMedGoogle Scholar
• Keele B. B., Jr., McCord J. M., Fridovich I. Superoxide dismutase fromEscherichia coli B; a new manganese-containing enzyme. J. Biol. Chem. 1970; 245: 6176
   PubMed Web of Science ®Google Scholar
• Lavelle F., Durosay P., Michelson A. M. Purification et proprietes de la superoxyde dismustase du champignon. Pleurotus olearius, Biochimie 1974; 56: 451
   PubMedGoogle Scholar
• Ravindranath S. D., Fridovich I. Isolation and characterization of a manganese-containing superoxide dismutase from yeast. J. Biol. Chem. 1975; 250: 6107
   PubMed Web of Science ®Google Scholar
• Salin M. L., Day E. D., Jr., Crapo J. D. Isolation and characterization of a manganese-containing superoxide dismutase from rat liver. Arch. Biochem. Biophys. 1978; 187: 223
   PubMed Web of Science ®Google Scholar
• Kirby T., Blum J., Khane I., Fridovich I. Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells. Arch. Biochem. Biophys. 1980; 201: 551
   PubMed Web of Science ®Google Scholar
• Kanematsu S., Asada K. Ferric and manganic superoxide dismutases in. Euglena gracilis, Arch. Biochem. Biophys. 1979; 195: 535
   PubMed Web of Science ®Google Scholar
• Bridges S. M., Salin M. L. Distribution of iron-containing superoxide dismutase in vascular plants. Plant Physiol. 1981; 68: 275
   PubMed Web of Science ®Google Scholar
• Gregory E. M., Dapper C. H. Chemical and physical differentiation of superoxide dismutases in anaerobes. J. Bacteriol. 1980; 144: 967
   PubMed Web of Science ®Google Scholar
• Steinman H. Superoxide dismutases: protein chemistry and structure-function relationships. Superoxide Dismutase, L. W. Oberley. CRC Press, Boca Raton, Fla. 1982; Vol. 1: 11
   Google Scholar
• Gregory E. M., Dapper C. H. Characterization of iron superoxide dismutase from. Bacteroides fragilis, Fed. Proc. 1982; 41: 889
   Google Scholar
• Meier B., Barra D., Bossa F., Calabrese L., Rotilio G. Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied. J. Biol. Chem. 1982; 257: 13977
   PubMed Web of Science ®Google Scholar
• Ichihara K., Kasoaka I., Kusunose E., Kusunose M. A manganese and iron containing superoxide dismutase from. Rhodococcus bronchialis, J. Gen. Appl. Microbiol. 1980; 26: 387
   Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Enzymatic defenses against the toxicity of oxygen and of streptonigrin inEscherichia coli K12. J. Bacteriol. 1977; 129: 1574
   PubMed Web of Science ®Google Scholar
• Dougherty H. W., Sadowski S. J., Baker E. E. A new iron-containing superoxide dismutase from. Escherichia coli, J. Biol. Chem. 1978; 253: 5220
   PubMed Web of Science ®Google Scholar
• Marklund S. L., Holme E., Hellner L. Superoxide dismutase in extracellular fluids. Clin. Chim. Acta 1982; 126: 41
   PubMed Web of Science ®Google Scholar
• Marklund S. L. Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. U.S.A. 1982; 79: 7634
   PubMed Web of Science ®Google Scholar
• Asada K., Yoshikawa K., Takahashi M., Maeda Y., Enmanji K. Superoxide dismutases from a blue-green alga. Plectonema boryanum, J. Biol. Chem. 1975; 250: 2801
   PubMed Web of Science ®Google Scholar
• Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 1975; 14: 5294
   Web of Science ®Google Scholar
• Kono Y., Fridovich I. Superoxide radical inhibits catalase. J. Biol. Chem. 1982; 257: 5751
   PubMed Web of Science ®Google Scholar
• Odajima T., Yamazaki I. Myeloperoxidase of the leukocyte of normal blood. III. The reaction of ferric myeloperoxidase with superoxide anion. Biochim. Biophys. Acta 1972; 284: 355
   PubMedGoogle Scholar
• Rotilio G., Bray R. C., Fielden E. M. A pulse radiolysis study of superoxide dismutase. Biochim. Biophys. Acta 1972; 268: 605
   PubMed Web of Science ®Google Scholar
• Misra H. P., Fridovich I. Inhibition of superoxide dismutases by azide. Arch. Biochem. Biophys. 1978; 189: 317
   PubMed Web of Science ®Google Scholar
• Heikkila R. E., Cabbat F. S., Cohen G. In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J. Biol. Chem. 1976; 251: 2182
   PubMed Web of Science ®Google Scholar
• Pottathil R., Chandrabose K. A., Cuatrecasas P., Lang D. J. Establishment of the interferonmediated antiviral state: possible role of superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 3343
   PubMed Web of Science ®Google Scholar
• Goldberg B., Stern A. Superoxide anion as a mediator of drug-induced oxidative hemolysis. J. Biol. Chem. 1976; 251: 6468
   PubMed Web of Science ®Google Scholar
• McCord J. M., Keele B. B., Jr., Fridovich I. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 1971; 68: 1024
   PubMed Web of Science ®Google Scholar
• Lindmark D. G., Muller M. Superoxide dismutase in the anaerobic flagellatesTritrichomonas foetus and Monocercomonas sp. J. Biol. Chem. 1974; 249: 4634
   PubMed Web of Science ®Google Scholar
• Hewitt J., Morris J. G. Superoxide dismutase in some obligately anaerobic bacteria. FEBS Lett. 1975; 50: 315
   PubMed Web of Science ®Google Scholar
• Carlsson J., Wrethen J., Beckman G. Superoxide dismutase in bacteroides species. J. Clin. Microbiol. 1977; 6: 280
   PubMed Web of Science ®Google Scholar
• Kirby T. W., Lancaster J. R., Jr., Fridovich I. Isolation and characterization of the iron-containing superoxide dismutase of. Methanobacterium bryantii, Arch. Biochem. Biophys. 1981; 210: 140
   PubMed Web of Science ®Google Scholar
• Uesugi I., Yajima M. Oxygen and strictly anaerobic intestinal bacteria. II. Oxygen metabolism in strictly anaerobic bacteria. Z. Allg. Microbiol. 1978; 18: 593
   PubMedGoogle Scholar
• Tally F. P., Goldin B. R., Jacobus N. V., Gorbach S. L. Superoxide dismutase in anaerobic bacteria of clinical significance. Infect. Immunol. 1977; 16: 20
   PubMed Web of Science ®Google Scholar
• Lynch R. E., Cole B. C. Mycoplasma pneumoniae: a prokaryote which consumes oxygen and generates superoxide but which lacks superoxide dismutase. Biochem. Biophys. Res. Commun. 1980; 96: 98
   PubMed Web of Science ®Google Scholar
• Norrod P., Morse S. A. Absence of superoxide dismutase in some strains of. Neisseria gonorrhoeae, Biochem. Biophys. Res. Commun. 1979; 90: 1287
   PubMed Web of Science ®Google Scholar
• Archibald F. S., Fridovich I. Manganese and defenses against oxygen toxicity in. Lactobacillus plantarum, J. Bacteriol. 1981; 145: 442
   PubMed Web of Science ®Google Scholar
• Archibald F. S., Fridovich I. Manganese, superoxide dismutase, and oxygen tolerance in some lactic acid bacteria. J. Bacteriol. 1981; 146: 928
   PubMed Web of Science ®Google Scholar
• Archibald F. S., Fridovich I. The scavenging of superoxide radical by manganous complexes. in vitro, Arch. Biochem. Biophys. 1982; 214: 452
   PubMed Web of Science ®Google Scholar
• Pasternack R. F., Halliwell B. Superoxide dismutase activities of an iron porphyrin and other iron complexes. J. Am. Chem. Soc. 1979; 101: 1026
   Web of Science ®Google Scholar
• Leuthauser S. W. C., Oberley L. W., Oberley T. D., Sorenson J. R. J., Ramakrishna K. Antitumor effect of a copper coordination compound with superoxide dismutase-like activity. J. Natl. Cancer Inst. 1981; 66: 1077
   PubMedGoogle Scholar
• Kimura E., Sakonaka A., Nakamoto M. Superoxide dismutase activity of macrocyclic polyamine complexes. Biochim. Biophys. Acta 1981; 678: 172
   PubMed Web of Science ®Google Scholar
• Halliwell B. The superoxide dismutase activity of iron complexes. FEBS Lett. 1975; 56: 34
   PubMed Web of Science ®Google Scholar
• Younes M., Weser U. Superoxide dismutase activity of copper-penicillamine: possible involvement of Cu(I) stabilized sulphur radical. Biochem. Biophys. Res. Commun. 1977; 78: 1247
   PubMed Web of Science ®Google Scholar
• Robertson P., Jr., Fridovich I. Does copper-D-penicillamine catalyze the dismutation of O2-. Arch. Biochem. Biophys. 1980; 203: 830
   PubMed Web of Science ®Google Scholar
• DiGuiseppi J., Fridovich I. Putative superoxide dismutase activity of iron-EDTA: a reexamination. Arch. Biochem. Biophys. 1980; 203: 145
   PubMed Web of Science ®Google Scholar
• Butler J., Halliwell B. Reaction of iron-EDTA chelates with the superoxide radical. Arch. Biochem. Biophys. 1982; 218: 174
   PubMed Web of Science ®Google Scholar
• Wardman P. Specificity of superoxide dismutase in catalyzing redox reactions: a pulse radiolysis study. Stud. Phys. Theor. Chem. 1979; 6: 189
   Google Scholar
• O'Neill P., Fielden E. M. Pulse radiolysis investigation of the interaction of bovine superoxide dismutase with organic free radicals. Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase, J. V. Bannister, H. A. O. Hill. Elsevier/North-Holland, New York 1980; 357
   Google Scholar
• Gregory E. M., Fridovich I. Induction of superoxide dismutase by molecular oxygen. J. Bacteriol. 1973; 114: 543
   PubMed Web of Science ®Google Scholar
• Welch D. F., Sword C. P., Brehm S., Dusanic D. Relationship between superoxide dismutase and pathogenic mechanisms of. Listeria monocytogenes, Infect. Immunol. 1979; 23: 863
   PubMed Web of Science ®Google Scholar
• Ghosh S., Chatterjee G. C. Superoxide dismutase activity inVibrio eltor in relation to oxygen toxicity and bactericidal action of nitrofurantoin. J. Gen. Appl. Microbiol. 1979; 25: 367
   Web of Science ®Google Scholar
• Privalle C. T., Gregory E. M. Superoxide dismutase and O2 lethality in. Bacteroides fragilis, J. Bacteriol. 1979; 138: 139
   PubMed Web of Science ®Google Scholar
• Stowers M. D., Elkan G. H. An inducible iron-containing superoxide dismutase in. Rhizobium japonicum, Can. J. Microbiol. 1981; 27: 1202
   Web of Science ®Google Scholar
• Moody C. S., Hassan H. M. Mutagenicity of oxygen free radicals. Proc. Natl. Acad. Sci. U.S.A. 1982; 79: 2855
   PubMed Web of Science ®Google Scholar
• Samah O. A., Wimpenny J. W. T. Some effects of oxygen on the physiology ofSelenomonas ruminantium WPL 151/1 grown in continuous culture. J. Gen. Microbiol. 1982; 128: 355
   Google Scholar
• DiGuiseppi J., Fridovich I. Oxygen toxicity inStreptococcus sanguis. The relative importance of superoxide and hydroxyl radicals. J. Biol. Chem. 1982; 257: 4046
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Physiological function of superoxide dismutase in glucose-limited chemostat cultures of. Escherichia coli, J. Bacteriol. 1977; 130: 805
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Regulation of superoxide dismutase synthesis inEscherichia coli: glucose effect. J. Bacteriol. 1977; 132: 505
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds. Arch. Biochem. Biophys. 1979; 196: 385
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Superoxide radical and the oxygen enhancement of the toxicity of paraquat in. Escherichia coli, J. Biol. Chem. 1978; 253: 8143
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Regulation of the synthesis of superoxide dismutase inEscherichia coli. Induction by methyl viologen. J. Biol. Chem. 1977; 252: 7667
   PubMed Web of Science ®Google Scholar
• Blum J., Fridovich I. Superoxide, hydrogen peroxide and oxygen toxicity in two free-living nematode species. Arch. Biochem. Biophys, in press
   Google Scholar
• Housset B., Junod A. F. Enzyme response of cultured endothelial cells to hyperoxia. Bull. Eur. Physiopathol. Resp. 1981; 17: 107, Suppl.
   PubMedGoogle Scholar
• Crapo J. D., Tierney D. F. Superoxide dismutase and pulmonary oxygen toxicity. Am. J. Physiol. 1974; 226: 1401
   PubMed Web of Science ®Google Scholar
• Stevens J. B., Autor A. P. Induction of superoxide dismutase by oxygen in neonatal rat lung. J. Biol. Chem. 1977; 252: 3509
   PubMed Web of Science ®Google Scholar
• Morris S. M., Albright J. T. Superoxide dismutase, catalase, and glutathione peroxidase in the swim bladder of the physoclistous fishOpsanus tau L. Cell Tissue Res. 1981; 220: 739
   PubMed Web of Science ®Google Scholar
• Dykens J. A., Shick J. M. Oxygen production by endosymbiotic algae controls superoxide dismutase activity in their animal host. Nature (London) 1982; 297: 579
   Web of Science ®Google Scholar
• Asada K., Kanematsu S., Takahashi M., Kono Y. Superoxide dismutases in photosynthetic organisms. Adv. Exp. Med. Biol. 1976; 74: 551
   PubMedGoogle Scholar
• Fuller E. C., Crist R. H. The rate of oxidation of sulfite ions by oxygen. J. Am. Chem. Soc. 1941; 63: 1644
   Google Scholar
• Hayon E., Treinin A., Wilf J. Electronic spectra, photochemistry and autoxidation mechanism of the sulfite-bisulfite-pyrosulfite systems. The SO2-, SO3-, SO4- and SO5- radicals. J. Am. Chem. Soc. 1972; 94: 47
   Web of Science ®Google Scholar
• Forman H. J., Fisher A. B. Antioxidant defenses. Oxygen and Living Processes, D. L. Gilbert. Springer-Verlag, New York 1981; 235
   Google Scholar
• Chen L. H., Thacker R. R., Chow C. K. Tissue anti-oxidant status and related enzymes in rats with long-term vitamin E deficiency. Nutr. Rep. Int. 1980; 22: 873
   Google Scholar
• Shatzman A. R., Kosman D. J. The utilization of copper and its role in the biosynthesis of copper-containing proteins in the fungus. Dactylium dendroides, Biochim. Biophys. Acta 1978; 544: 163
   PubMedGoogle Scholar
• De Rosa G., Keen C. L., Leach R. M., Hurley L. S. Regulation of superoxide dismutase activity by dietary manganese. J. Nutr. 1980; 110: 795
   PubMed Web of Science ®Google Scholar
• Del Rio L. A., Sevilla F., Gomez M., Yance J., Lopez J. Superoxide dismutase: an enzyme system for the study of micronutrient interaction in plants. Planta 1978; 140: 221
   PubMed Web of Science ®Google Scholar
• Gregory E. M., Fridovich I. Oxygen toxicity and the superoxide dismutase. J. Bacteriol. 1973; 114: 1193
   PubMed Web of Science ®Google Scholar
• Friedberg D., Fine M., Oren A. Effect of oxygen on the cyanobacterium. Oscillatoria limnetica, Arch. Microbiol. 1979; 123: 311
   Web of Science ®Google Scholar
• Hassan H. M., Fridovich I. Mechanism of the antibiotic action of pyocyanine. J. Bacteriol. 1980; 141: 156
   PubMed Web of Science ®Google Scholar
• Lavelle F., Michelson A. M., Dimitrijevic L. Biological protection by superoxide dismutase. Biochem. Biophys. Res. Commun. 1973; 55: 350
   PubMed Web of Science ®Google Scholar
• Babior B. M., Curnutte J. T., Kipnes R. S. Biological defense mechanisms. Evidence for the participation of superoxide in bacterial killing by xanthine oxidase. J. Lab. Clin. Med. 1975; 85: 235
   PubMed Web of Science ®Google Scholar
• Kellogg E. W., Yost M. G., Barthakur N., Kreuger A. P. Superoxide involvement in the bactericidal effects of negative air ionisers on. Staphylococcus albus, Nature (London) 1979; 281: 400
   PubMed Web of Science ®Google Scholar
• Cope P. A., Dawson M. The effects of interactions between sodium ascorbate and superoxide radicals generated by hypoxanthine and xanthine oxidase on 3T3 cells. Cell Biol. Int. Rep. 1980; 4: 748
   Google Scholar
• Michelson A. M., Buckingham M. E. Effects of superoxide radicals on myoblast growth and differentiation. Biochem. Biophys. Res. Commun. 1974; 58: 1079
   PubMed Web of Science ®Google Scholar
• Petkau A., Kelly K., Chelack W. S., Pleskach S. D., Barefoot C., Meeker B. E. Radioprotection of bone marrow stem cells by superoxide dismutase. Biochem. Biophys. Res. Commun. 1975; 67: 1167
   PubMed Web of Science ®Google Scholar
• Van Hemmen J. J., Meuling W. J. A. Inactivation of biologically active DNA by γ-ray-induced superoxide radicals and their dismutation products singlet molecular oxygen and hydrogen peroxide. Biochim. Biophys. Acta 1975; 402: 113
   PubMedGoogle Scholar
• Petkau A., Chelack W. S. Radioprotective effect of superoxide dismutase on model phospholipid membranes. Biochim. Biophys. Acta 1976; 433: 445
   PubMed Web of Science ®Google Scholar
• Nordenson I., Beckman G., Beckman L. The effect of superoxide dismutase and catalase on radiation-induced chromosome breaks. Hereditas 1976; 82: 125
   PubMed Web of Science ®Google Scholar
• Petkau A., Chelack W. S., Pleskach S. D. Protection of postirradiated mice by superoxide dismutase. Int. J. Radiat. Biol. 1976; 29: 297
   Web of Science ®Google Scholar
• Oberley L. W., Lindgren L. A., Baker S. A., Stevens R. H. Superoxide ion as the cause of the oxygen effect. Radiat. Res. 1976; 68: 320
   PubMed Web of Science ®Google Scholar
• McLennan G., Oberley L. W., Autor A. P. The role of oxygen-derived free radicals in radiation-induced damage and death of nondividing eukaryotic cells. Radiat. Res. 1980; 84: 122
   PubMed Web of Science ®Google Scholar
• Emerit I., Michelson A. M. Chromosome instability in human and murine autoimmune disease: anticlastogenic effect of superoxide dismutase. Acta Physiol. Scand. 1980; 492: 59, Suppl.
   Google Scholar
• Emerit I., Levy A., Michelson A. M. Effect of superoxide dismutase on the chromosomal instability of New Zealand black mice. Cytogenet. Cell Genet. 1981; 30: 65
   PubMedGoogle Scholar
• Nagasawa H., Little J. B. Factors influencing the induction of sister chromatid exchanges in mammalian cells by 12-o-tetradecanoyl-phorbol-13-acetate. Carcinogenesis 1981; 2: 601
   PubMed Web of Science ®Google Scholar
• Birnboim H. C. DNA strand breakage in human leukocytes exposed to a tumor promoter, phorbol myristate acetate. Science 1982; 215: 1247
   PubMed Web of Science ®Google Scholar
• Brawn K., Fridovich I. DNA strand scission by enzymically generated oxygen radicals. Arch. Biochem. Biophys. 1981; 206: 414
   PubMed Web of Science ®Google Scholar
• Lesko S. A., Drocourt J. L., Yang S. U. Deoxyribonucleic acid-protein and deoxyribonucleic acid interstrand cross-links induced in isolated chromatin by hydrogen peroxide and ferrous ethylenedi-aminetetraacetate chelates. Biochemistry 1982; 21: 5010
   PubMed Web of Science ®Google Scholar
• Weitzman S. A., Stossel T. P. Mutation caused by human phagocytes. Science 1981; 212: 546
   PubMed Web of Science ®Google Scholar
• Yamaguchi T. Mutagenicity of low molecular substances in various superoxide generating systems. Agric. Biol. Chem. 1981; 45: 327
   Web of Science ®Google Scholar
• Emerit I., Cerutti P. A. Tumor promotor phorbol-12-myristate-13-acetate induces chromosomal damage via indirect action. Nature (London) 1981; 293: 144
   PubMed Web of Science ®Google Scholar
• Docampo R., Moreno S. N. J., Stoppani A. O. M. Nitrofuran enhancement of microsomal electron transport, superoxide anion production and lipid peroxidation. Arch. Biochem. Biophys. 1981; 207: 316
   PubMed Web of Science ®Google Scholar
• Greenstock C. L., Miller R. W. The oxidation of tiron by superoxide anion: kinetics of the reaction in aqueous solution and in chloroplasts. Biochim. Biophys. Acta 1975; 396: 11
   PubMedGoogle Scholar
• Lynch R. E., Lee G. R., Cartwright G. E. Inhibition by superoxide dismutase of methemoglobin formation from oxyhemoglobin. J. Biol. Chem. 1976; 251: 1015
   PubMed Web of Science ®Google Scholar
• Elstner E. F., Heupel A. Inhibition of nitrite formation from hydroxylammonium-chloride: a simple assay for superoxide dismutase. Anal. Biochem. 1976; 70: 616
   PubMed Web of Science ®Google Scholar
• Misra H. P., Fridovich I. The oxidation of phenylhydrazine: superoxide and mechanism. Biochemistry 1976; 15: 681
   PubMed Web of Science ®Google Scholar
• Nishikimi M., Yamada H., Yagi K. Oxidation by superoxide of tocopherols dispersed in aqueous media with deoxycholate. Biochim. Biophys. Acta 1980; 627: 101
   PubMed Web of Science ®Google Scholar
• Hassan H. M., Dougherty H., Fridovich I. Inhibitors of superoxide dismutases: a cautionary tale. Arch. Biochem. Biophys. 1980; 199: 349
   PubMed Web of Science ®Google Scholar
• Li J. R., Kim D. N. Effects of superoxide dismutase on cholesterol 7α-hydroxylation in swine. Steroids 1980; 35: 459
   PubMed Web of Science ®Google Scholar
• Robertson P., Jr., Fridovich I. A reaction of the superoxide radical with tetrapyrroles. Arch. Biochem. Biophys. 1982; 213: 353
   PubMed Web of Science ®Google Scholar
• Thomas M. J., Mehl K. S., Pryor W. A. The role of superoxide in xanthine oxidase-induced autoxidation of linoleic acid. J. Biol. Chem. 1982; 257: 8343
   PubMed Web of Science ®Google Scholar
• Frimer A. A., Rosenthal I., Hoz S. The reaction of superoxide anion radical with electron poor olefins. Tet. Lett. 1977; 52: 4631
   Google Scholar
• Asami S., Akazawa T. Enzymic formation of glycolate inChromatium. Role of superoxide radical in a transketolase-type mechanism. Biochemistry 1977; 16: 2202
   PubMed Web of Science ®Google Scholar
• Schneider K., Schlegel H. G. Production of superoxide radicals by soluble hydrogenase fromAlcaligenes eutrophus H16. Biochem. J. 1981; 193: 99
   PubMed Web of Science ®Google Scholar
• Bielski B. H. J., Chan P. C. Kinetic study by pulse radiolysis of the lactate dehydrogenase-catalyzed chain oxidation of nicotinamide adenine dinucleotide by HO2 and O2- radicals. J. Biol. Chem. 1975; 250: 318
   PubMed Web of Science ®Google Scholar
• Ross F., Ross A. B. Selected specific rates of reactions of transients from water in aqueous solution. III. Hydroxyl radical and perhydroxyl radical and their radical ions, NSRDS-NBS 59. U.S. Government Printing Office, Washington, D.C. 1977
   Google Scholar
• Gebicki J., Bielski B. H. J. Comparison of the capacities of the perhydroxyl and the superoxide radicals to initiate chain oxidation of linoleic acid. J. Am. Chem. Soc. 1981; 103: 7020
   Web of Science ®Google Scholar
• Trauble H. Membrane electrostatics. Structure of Biological Membranes, S. Abrahamsson, I. Pascher. Plenum Press, New York 1976; 509
   Google Scholar
• Talcott R. E., Shu H., Wei E. T. Lipid peroxidation and paraquat toxicity. Fed. Proc. 1977; 36: 998
   Google Scholar
• Beauchamp C., Fridovich I. A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase. J. Biol. Chem. 1970; 245: 4641
   PubMed Web of Science ®Google Scholar
• Haber F., Weiss J. The catalytic decomposition of hydrogen peroxide by iron salts. Proc. R. Soc. London Ser. A 1934; 147: 332
   Google Scholar
• Gibian M. J., Ungermann T. The unlikelihood of an electron-transfer (Haber-Weiss) reaction between superoxide and peroxides. J. Am. Chem. Soc. 1979; 101: 1291
   Web of Science ®Google Scholar
• Rigo A., Stevanato R., Rotilio G., Finazzi-Agro A. An attempt to evaluate the rate of the Haber-Weiss reaction by using OH radical scavengers. FEBS Lett. 1977; 80: 130
   PubMed Web of Science ®Google Scholar
• McClune G. J., Fee J. A. Stopped flow spectrophotometric observation of superoxide dismutation in aqueous solution. FEBS Lett. 1976; 67: 294
   PubMed Web of Science ®Google Scholar
• Halliwell B. An attempt to demonstrate a reaction between superoxide and hydrogen peroxide. FEBS Lett. 1976; 72: 8
   PubMed Web of Science ®Google Scholar
• Weinstein J., Bielski B. H. J. Kinetics of the interaction of HO2 and O2- radicals with hydrogen peroxide. The Haber-Weiss reaction. J. Am. Chem. Soc. 1979; 101: 58
   Web of Science ®Google Scholar
• Masuda T., Nakano S., Kondo M. Reactivities of enzyme toward hydroxyl radicals. J. Radiat. Res. 1974; 15: 171
   PubMedGoogle Scholar
• Nohl H., Breuninger V., Hegner D. Influence of mitochondrial radical formation on energy-linked respiration. Eur. J. Biochem. 1978; 90: 385
   PubMedGoogle Scholar
• Schuh J., Fairclough G. F., Jr., Haschemeyer R. H. Oxygen-mediated heterogeneity of apo-low-density lipoprotein. Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 3173
   PubMed Web of Science ®Google Scholar
• Tozum S. R. D., Gallon J. R. The effects of methyl viologen onGloeocapsa sp. LB795 and their relationship to the inhibition of acetylene reduction (nitrogen fixation) by oxygen. J. Gen. Microbiol. 1979; 111: 313
   Google Scholar
• Meneghini R., Hoffmann M. E. The damaging action of hydrogen peroxide on DNA of human fibroblasts is mediated by a non-dialyzable compound. Biochim. Biophys. Acta 1980; 608: 167
   PubMedGoogle Scholar
• Fischer L. J., Hamburger S. A. Inhibition of alloxan action in isolated pancreatic islets by superoxide dismutase, catalase, and a metal chelator. Diabetes 1980; 29: 213
   PubMed Web of Science ®Google Scholar
• De Vries J., Verboom C. N. Effects of scavengers of superoxide radicals, hydrogen peroxide, singlet oxygen and hydroxyl radicals on malondialdehyde generation from arachidonic acid by bovine seminal vesicle microsomes. Experientia 1980; 36: 1339
   PubMedGoogle Scholar
• Videla L. A., Fernandez V., Ugarte G., Valenzuela A. Effect of acute ethanol intoxication on the content of reduced glutathione of the liver in relation to its lipoperoxidative capacity in the rat. FEBS Lett. 1980; 111: 6
   PubMed Web of Science ®Google Scholar
• Valenzuela A., Fernandez N., Fernandez V., Ugarte G., Videla L. A. Effect of acute ethanol ingestion on lipoperoxidation and on the activity of the enzymes related to peroxide metabolism in rat liver. FEBS Lett. 1980; 111: 11
   PubMed Web of Science ®Google Scholar
• Perez H. D., Weksler B. B., Goldstein I. M. Generation of a chemotactic lipid from arachidonic acid by exposure to a superoxide-generating system. Inflammation 1980; 4: 313
   PubMed Web of Science ®Google Scholar
• Rosen H., Klebanoff S. J. Role of iron and ethylenediaminetetraacetic acid in the bactericidal activity of a superoxide anion-generating system. Arch. Biochem. Biophys. 1981; 208: 512
   PubMed Web of Science ®Google Scholar
• Heikkila R. E., Cabbat F. S. Inhibition of iron-stimulated catecholamine degradation by the iron-chelators DETAPAC and Desferal. Potentially useful laboratory agents. Biochem. Pharm. 1981; 30: 2945
   PubMed Web of Science ®Google Scholar
• Bradley M. O., Erickson L. C. Comparison of the effects of hydrogen peroxide and X-ray irradiation on toxicity, mutation, and DNA damage/repair in mammalian cells (V-79). Biochim. Biophys. Acta 1981; 654: 135
   PubMed Web of Science ®Google Scholar
• Fujita S., Steenken S. Pattern of OH radical addition to uracil and methyl- and carboxyl-substituted uracils. Electron transfer of OH adducts with N,N,N′,N′-tetramethyl-p-phenylenediamine and tetranitromethane. J. Am. Chem. Soc. 1981; 103: 2540
   Web of Science ®Google Scholar
• Taniguchi M., Aikawa M., Sakagami T. A simple and effective method for homolysis with a hypoxanthine-xanthine oxidase system and alteration of erythrocyte phospholipid composition during the hemolysis. J. Biochem. 1981; 89: 795
   PubMed Web of Science ®Google Scholar
• Fridovich S. E., Porter N. A. Oxidation of arachidonic acid in micelles by superoxide and hydrogen peroxide. J. Biol. Chem. 1981; 256: 260
   PubMed Web of Science ®Google Scholar
• Repine J. E., Fox R. B., Berger E. M. Hydrogen peroxide killsStaphylococcus aureus by reacting with staphylococcal iron to form hydroxyl radical. J. Biol. Chem. 1981; 256: 7094
   PubMed Web of Science ®Google Scholar
• Wong S. F., Halliwell B., Richmond R., Skowroneck W. R. The role of superoxide and hydroxyl radicals in the degradation of hyaluronic acid induced by metal ions and by ascorbic acid. J. Inorg. Biochem. 1981; 14: 127
   PubMed Web of Science ®Google Scholar
• Trelstad R. L., Lawley K. R., Holmes L. B. Nonenzymatic hydroxylations of proline and lysine by reduced oxygen derivatives. Nature (London) 1981; 289: 310
   PubMed Web of Science ®Google Scholar
• Repine J. R., Pfenninger O. W., Talmage D., Berger E. M., Pettijohn D. E. Dimethyl sulfoxide prevents DNA nicking mediated by ionizing radiation or iron/hydrogen peroxide-generated hydroxyl radical. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 1001
   PubMed Web of Science ®Google Scholar
• Hertzberg R. P., Dervan P. B. Cleavage of double helical DNA by (methidiumpropyl-EDTA) iron (II). J. Am. Chem. Soc. 1982; 104: 312
   Web of Science ®Google Scholar
• Gutteridge J. M. C. Free radical damage to lipids, amino acids, carbohydrates and nucleic acids determined by thiobarbituric acid reactivity. Int. J. Biochem. 1982; 14: 649
   PubMedGoogle Scholar
• Weiss S. J. Neutrophil-mediated methemoglobin formation in the etythrocyte. The role of superoxide and hydrogen peroxide. J. Biol. Chem. 1982; 257: 2947
   PubMed Web of Science ®Google Scholar
• Forney L. J., Reddy C. A., Tien M., Aust S. D. The involvement of hydroxyl radical derived from hydrogen peroxide in lignin degradation by the white rot fungus. Phanerochaete chrysosporium, J. Biol. Chem. 1982; 257: 11455
   PubMed Web of Science ®Google Scholar
• McCord J. M., Day E. D., Jr. Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex. FEBS Lett. 1978; 86: 139
   PubMed Web of Science ®Google Scholar
• Fenton H. J. H. Oxidation of tartaric acid in presence of iron. J. Chem. Soc. 1894; 65: 899
   Google Scholar
• DiGuiseppi J., Fridovich I. Ethylene from 2-keto-4-thiomethyl butyric acid: the Haber-Weiss reaction. Arch. Biochem. Biophys. 1980; 205: 323
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C., Richmond R., Halliwell B. Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine. Biochem. J. 1979; 184: 469
   PubMed Web of Science ®Google Scholar
• Ambruso D. R., Johnston R. B., Jr. Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system. J. Clin. Invest. 1981; 67: 352
   PubMed Web of Science ®Google Scholar
• Bannister J. V., Bannister W. H., Hill H. A. O., Thornalley P. J. Enhanced production of hydroxyl radicals by the xanthine oxidase reaction in the presence of lactoferrin. Biochim. Biophys. Acta 1982; 715: 116
   PubMed Web of Science ®Google Scholar
• Kono Y., Sugiura Y. Electron spin resonance studies on the oxidation of rifamycin SV catalyzed by metal ions. J. Biochem. 1982; 91: 397
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C. Identification of malondialdehyde as the TBA-reactant formed by bleomycin-iron free radical damage to DNA. FEBS Lett. 1979; 105: 278
   PubMed Web of Science ®Google Scholar
• Sugiura Y., Ogawa S., Morishima I. Unusual interaction of iron-bleomycin with cyanide. J. Am. Chem. Soc. 1980; 102: 7944
   Web of Science ®Google Scholar
• Kuramochi H., Takahashi K., Takita T., Umezawa H. An active intermediate formed in the reaction of bleomycin-Fe(II) complex with oxygen. J. Antibiot. 1981; 34: 576
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C., Rowley D. A., Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Biochem. J. 1981; 199: 263
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C., Rowley D. A., Halliwell B. Superoxide-dependent formation of hydroxyl radicals and lipid peroxidation in the presence of iron salts. Biochem. J. 1982; 206: 605
   PubMed Web of Science ®Google Scholar
• Milas N. A., Kurz P. F., Anslow W. P., Jr. The photochemical addition of hydrogen peroxide to the double bonds. J. Am. Chem. Soc. 1937; 59: 543
   Google Scholar
• Cahill A. E., Taube H. The use of heavy oxygen in the study of reactions of hydrogen peoxide. J. Am. Chem. Soc. 1952; 74: 2312
   Web of Science ®Google Scholar
• Gutteridge J. M. C., Wilkins S. Copper-dependent hydroxyl radical damage to ascorbic acid. Formation of a thiobabituric acid-reaction product. FEBS Lett. 1982; 137: 327
   PubMed Web of Science ®Google Scholar
• Nohl H., Jordan W., Hegner D. Mitochondrial formation of OH radicals by an ubisemiquinone-dependent reaction; an alternative pathway to the iron-catalysed Haber-Weiss cycle. Hoppe-Seyler's Z. Physiol. Chem. 1982; 363: 599
   PubMedGoogle Scholar
• Winterbourn C. C. Evidence for the production of hydroxyl radicals from the adriamycin semiquinone and H2O2. FEBS Lett. 1981; 136: 89
   Web of Science ®Google Scholar
• Youngman R. J., Elstner E. F. Oxygen species in paraquat toxicity: the crypto-OH radical. FEBS Lett. 1981; 129: 265
   PubMed Web of Science ®Google Scholar
• Rowley D. A., Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of thiol compounds. FEBS Lett. 1982; 138: 33
   PubMed Web of Science ®Google Scholar
• Nohl H., Jordan W., Hegner D. Identification of free hydroxyl radicals in respiring rat heart mitochondria by spin trapping with the nitrone DMPO. FEBS Lett. 1981; 123: 241
   PubMed Web of Science ®Google Scholar
• Elstner E. F., Konze J. R. Light-dependent ethylene production by isolated chloroplasts. FEBS Lett. 1974; 45: 18
   PubMed Web of Science ®Google Scholar
• Konze J. R., Elstner E. F. Pyridoxal phosphate-dependent ethylene production from methionine by isolated chloroplasts. FEBS Lett. 1976; 66: 8
   Web of Science ®Google Scholar
• Cohen G., Cederbaum A. I. Chemical evidence for production of hydroxyl radicals during microsomal electron transfer. Science 1979; 204: 66
   PubMed Web of Science ®Google Scholar
• Cohen G., Cederbaum A. I. Microsomal metabolism of hydroxyl radical scavenging agents relationship to the microsomal oxidation of alcohols. Arch. Biochem. Biophys. 1980; 199: 438
   PubMed Web of Science ®Google Scholar
• Cederbaum A. I., Cohen G. Inhibition of the microsomal oxidation of ethanol and I-butanol by the free-radical, spin-trapping agent 5,5-dimethyl-1-pyrroline-1-oxide. Arch. Biochem. Biophys. 1980; 204: 397
   PubMed Web of Science ®Google Scholar
• Cederbaum A. I., Dicker E., Cohen G. Role of hydroxyl radicals in the iron-ethylenediamine-tetraacetic acid mediated stimulation of microsomal oxidation of ethanol. Biochemistry 1980; 19: 3698
   PubMed Web of Science ®Google Scholar
• Ingelman-Sundberg M., Ekstrom G. Aniline is hydroxylated by the cytochrome P-450-dependent hydroxyl radical-mediated oxygenation mechanism. Biochem. Biophys. Res. Commun. 1982; 106: 625
   PubMed Web of Science ®Google Scholar
• Weiss S. J., King G. W., LoBuglio A. F. Evidence for hydroxyl radical generation by human monocytes. J. Clin. Invest. 1977; 60: 370
   PubMed Web of Science ®Google Scholar
• Tauber A. I., Babior B. M. Evidence for hydroxyl radical production by human neutrophils. J. Clin. Invest. 1977; 60: 374
   PubMed Web of Science ®Google Scholar
• Weiss S. J., Rustagi P. K., LoBuglio A. F. Human granulocyte generation of hydroxyl radical. J. Exp. Med. 1978; 147: 316
   PubMed Web of Science ®Google Scholar
• Klebanoff S. J., Rosen H. Ethylene formation by polymorphonuclear leukocytes. Role of myeloperoxidase. J. Exp. Med. 1978; 148: 490
   PubMed Web of Science ®Google Scholar
• Repine J. E., Eaton J. W., Anders M. W., Hoidal J. R., Fox R. B. Generation of hydroxyl radical by enzymes, chemicals, and human phagocytes in vitro. Detection with the anti-inflammatory agent, dimethyl sulfoxide. J. Clin. Invest. 1979; 64: 1642
   PubMed Web of Science ®Google Scholar
• Sagone A. L., Jr., Decker M. A., Wells R. M., Democko C. A new method for the detection of hydroxyl radical production by phagocytic cells. Biochim. Biophys. Acta 1980; 628: 90
   PubMed Web of Science ®Google Scholar
• Heikkila R. E., Winston B., Cohen G. Alloxan-induced diabetes-evidence for hydroxyl radical as a cytotoxic intermediate. Biochem. Pharm. 1976; 25: 1085
   PubMed Web of Science ®Google Scholar
• Grankvist K., Marklund S., Taljedal I.-B. Superoxide dismutase is a prophylactic against alloxan diabetes. Nature (London) 1981; 294: 158
   PubMed Web of Science ®Google Scholar
• Grankvist K., Marklund S., Sehlin J., Taljedal I.-B. Superoxide dismutase, catalase and scavengers of hydroxyl radical protect against the toxic action of alloxan on pancreatic islet cells in vitro. Biochem. J. 1979; 182: 17
   PubMed Web of Science ®Google Scholar
• Fischer L. J., Hamburger S. A. Inhibition of alloxan action in isolated pancreatic islets by superoxide dismutase, catalase and a metal chelator. Diabetes 1980; 29: 213
   PubMed Web of Science ®Google Scholar
• Ishibashi F., Howard B. V. Alloxan and H2O2, action on glucose metabolism in cultured fibroblasts. J. Biol. Chem. 1981; 256: 12134
   PubMed Web of Science ®Google Scholar
• Dillard C. J., Kunert K. J., Tappel A. L. Effects of vitamin E, ascorbic acid and mannitol on alloxan-induced lipid peroxidation in rats. Arch. Biochem. Biophys. 1982; 216: 204
   PubMed Web of Science ®Google Scholar
• Klein S. M., Cohen G., Cederbaum A. I. Production of formaldehyde during metabolism of dimethyl sulfoxide by hydroxyl radical generating systems. Biochemistry 1981; 20: 6006
   PubMed Web of Science ®Google Scholar
• Menander-Hube K. B., Huber W. Orgotein, the drug version of bovine Cu-Zn superoxide dismutase. II. A summary account of clinical trials in man and animals. Superoxide and Superoxide Dismutases, A. M. Michelson, J. M. McCord, I. Fridovich. Academic Press, London 1977; 537
   Google Scholar
• McCord J. M. Free radicals and inflammation: protection of synovial fluid by superoxide dismutase. Science 1974; 185: 529
   PubMed Web of Science ®Google Scholar
• Salin M. L., McCord J. M. Free radicals and inflammation. Protection of phagocytosing leukocytes by superoxide dismutase. J. Clin. Invest. 1975; 56: 1319
   PubMed Web of Science ®Google Scholar
• Abuchowski A., McCoy J. R., Palczuk N. C., Van Es T., Davis F. F. Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J. Biol. Chem. 1977; 252: 3582
   PubMed Web of Science ®Google Scholar
• Sacks T., Moldow C. F., Craddock P. R., Bowers T. K., Jacob H. S. Oxygen radicals mediate endothelial cell damage by complement-stimulated granulocytes. An invitro model of immune vascular damage. J. Clin. Invest. 1978; 61: 1161
   PubMed Web of Science ®Google Scholar
• McCord J. M., Wong K. Phagocyte-produced free radicals: roles in cytotoxicity and inflammation. Ciba Found. Symp. 1979; 65: 343
   Google Scholar
• Blake D. R., Hall N. D., Bacon P. A., Dieppe P. A., Halliwell B., Gutteridge J. M. C. The importance of iron in rheumatoid disease. Lancet 1981; 21: 1142
   Google Scholar
• McCormick J. R., Harkin M. M., Johnson K. J., Ward P. A. Suppression by superoxide dismutase of immune-complex-induced pulmonary alveolitis and dermal inflammation. Am. J. Pathol. 1981; 102: 55
   PubMed Web of Science ®Google Scholar
• Petrone W. F., English D. K., Wong K., McCord J. M. Free radicals and inflammation: superoxide-dependent activation of a neutrophil chemotactic factor in plasma. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 1159
   PubMed Web of Science ®Google Scholar
• Goetzl E. J., Hill H. R., Gorman R. R. Unique aspects of the modulation of human neutrophil function by 12-L-hydroperoxy-5,8,10,14-eicosatetraenoic acid. Prostaglandins 1980; 19: 71
   PubMedGoogle Scholar
• Fridovich I. Hypoxia and oxygen toxicity. Cerebral Hypoxia and Its Consequences, Advances in Neurology, S. Fahn, J. N. Davis, L. P. Rowland. Raven Press, New York 1979; Vol. 26: 255
   Google Scholar
• Bailie M. B., Jolly S. R., Lucchesi B. R. Reduction of myocardial ischemic injury by superoxide dismutase plus catalase. Fed. Proc. 1982; 41: 1736
   Google Scholar
• Granger D. N., Rutili G., McCord J. M. Superoxide radicals in feline intestinal ischemia. Gastroenterology 1981; 81: 22
   PubMed Web of Science ®Google Scholar
• Parks D. A., Bulkley G. B., Granger D. N., Hamilton S. R., McCord J. M. Ischemic injury in the cat small intestine: role of superoxide radicals. Gastroenterology 1982; 82: 9
   PubMed Web of Science ®Google Scholar
• Parks D. A., Granger D. N., Bulkley G. B. Superoxide radicals and mucosal lesions of the ischemic small intestine. Fed. Proc 1982; 41: 1742
   Google Scholar
• Lin P.-F., Slate D. L., Lawyer F. C., Ruddle F. H. Assignment of the murine interferon sensitivity and cytoplasmic superoxide dismutase genes to chromosome 16. Science 1980; 209: 285
   PubMed Web of Science ®Google Scholar
• Peskin A. V., Koen Y. M., Zbarsky I. B. Superoxide dismutase and glutathione peroxidase activities in tumors. FEBS Lett. 1977; 78: 41
   PubMed Web of Science ®Google Scholar
• Oberley L. W., Bize I. B., Sahu S. K., Leuthauser S. W. H. C., Gruber H. E. Superoxide dismutase activity of normal murine liver, regenerating liver, and H6 hepatoma. J. Natl. Cancer Inst. 1978; 61: 375
   PubMedGoogle Scholar
• Bartkowiak A., Bartkowiak J. Superoxide dismutase and catalase activities in normal and cancerous tissues. Comp. Biochem. Physiol. 1981; 70B: 819
   Google Scholar
• Oberley L. W., Buettner G. R. Role of superoxide dismutase in cancer: a review. Cancer Res. 1979; 39: 1141
   PubMed Web of Science ®Google Scholar
• Reiss U., Gershon D. Rat-liver superoxide dismutase. Purification and age-related modifications. Eur. J. Biochem. 1976; 63: 617
   PubMedGoogle Scholar
• Massie H. R., Aiello V. R., Iodice A. A. Changes with age in copper and superoxide dismutase levels in brains of C57BL/6J mice. Mech. Ageing Dev. 1979; 10: 93
   PubMed Web of Science ®Google Scholar
• Kellogg E. W., III, Fridovich I. Superoxide dismutase in the rat and mouse as a function of age and longevity. J. Gerontol. 1976; 31: 405
   PubMedGoogle Scholar
• Tolmasoff J. M., Ono T., Cutler R. G. Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 2777
   PubMed Web of Science ®Google Scholar
• McArthur M. C., Sohal R. S. Relationship between metabolic rate, aging, lipid peroxidation, and fluorescent age pigment in milkweed bugOncopeltus fasciatus (Hemiptera). J. Gerontol. 1982; 37: 268
   PubMedGoogle Scholar
• Ragland S., Sohal R. S. Mating behavior, physical activity and life span in the adult housefly. Musca domestica, Exp. Gerontol. 1973; 8: 135
   PubMed Web of Science ®Google Scholar
• Sohal R. S. Metabolic rate, aging, and lipofuscin accumulation. Age Pigments, R. S. Sohal. Elsevier/North-Holland, Amsterdam 1981; 303
   Google Scholar
• Sohal R. S., Buchan P. B. Relationship between fluorescent age pigment, physiological age and physical activity in the housefly. Musca domestica, Mech. Ageing Dev. 1981; 15: 243
   PubMed Web of Science ®Google Scholar
• Packer L., Fuchr K. Low oxygen concentration extends the life-span of cultured human diploid cells. Nature (London) 1977; 267: 423
   PubMed Web of Science ®Google Scholar
• Pryor W. A. Free radicals in biology. The involvement of radical reactions in aging and carcinogenesis. Medicinal Chemistry, W. A. Pryor. Elsevier, New York 1977; Vol. 5: 331
   Google Scholar
• Miller D. S., Payne P. R. Longevity and protein intake. Exp. Gerontol. 1968; 3: 231
   PubMed Web of Science ®Google Scholar
• Barrows C. H., Jr., Kokkonen G. C. Diet and life extension in animal model systems. Age 1978; 1: 131
   Google Scholar
• Harmon D. The aging process. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 7124
   PubMed Web of Science ®Google Scholar