Abstract
One-electron reductions of dioxygen form superoxide ion, O —2 (Sawyer and Valentine, 1981). Although triplet dioxygen is a rather poor one-electron oxidant, superoxide ion is a strong one-electron oxidant if protons are available.
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References
Abernethy, J. L., Steinman, H. M., and Hill, R. L., 1974. Bovine erythrocyte superoxide dismutase: Subunit structure and sequence location of the intrasubunit disulfide bond, J Biol. Chem. 249: 7339–7347.
Anbar, M., Meyerstein, D., and Neta, P., 1966. Reactivity of aliphatic compounds towards hydroxyl radicals, J. Am. Chem. Soc. (B) 1966: 742–747.
Andrews, L., 1968. Matrix infrared spectrum and bonding in the lithium superoxide molecule, L1O2, J. Am. Chem. Soc. 103: 4965–4966.
Aubry, J. M., Rigaudy, J., Ferradini, C., and Pucheault, J., 1981. A search for singlet oxygen in disproportionation of superoxide anion, J. Am. Chem. Soc. 103: 4965–4966.
Audley, G. J., Baulch, D. L., and Campbell, I. M., 1981. Gas-phase reactions of hydroxyl radicals with aldehyde in flowing H202 + N02 + CO mixtures, J. Chem. Soc. Faraday Trans. 1 1981: 2451–2549.
Aust, S. E., Roerig, D. L., and Pederson, T. C. P., 1972. Evidence for superoxide generation by NADPH-cytochrome c reductase of rat liver microsomes, Biochem. Biophys. Res. Commun. 47: 1133–1137.
Azzi, A., Montecrucco, C. and Richiter, C., 1975. The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes, Biochem. Biophys. Res. Commun. 65: 597–603.
Bannister, J. V., Bannister, W. H., Bray, R. C., Fielden, E. M., Roberts, P. B., and Rotilio, G., 1973. The superoxide dismutase activity of human erythrocuprein, FEBS Lett. 32: 303–306.
Beauchamp, C., and Fridovich, L., 1970. A mechanism of production of ethylene from methional: The generation of hydroxyl radical by xanthine oxidase, J. Biol. Chem. 245: 4641–4646.
Behar, D., Czapski, G., Rabini, J., Dorfman, L. M., and Schwarz, H., 1970. The acid dissociation constant and decay kinetics of the perhydroxyl radical, J. Phys. Chem. 74: 3209–3213.
Bellus, D., 1979. Physical quenchers of singlet molecular oxygen, in Advances in Photochemistry, Vol. 11, J. M. Pitts, Jr., G. S. Hammond, K. Gollnick, and D. Grosjean (eds.), John Wiley, New York, pp. 105–205.
Bielski, B. H. J., 1978. Reevaluation of the spectral and kinetic properties of HO2 and O2 free radicals, Photochem. Photobiol. 28: 645–649.
Bielski, B. H. J., and Allen, A. D., 1977. Mechanism of the disproportionation of superoxide radicals, J. Phys. Chem. 81: 1048–1050.
Bielski, B. H. J., and Richter, H. W., 1977. A study of the superoxide radical chemistry by stopped-flow radiology and radiation-induced oxygen consumption, J. Am. Chem. Soc. 99: 3019–3023.
Bielski, B. H. J., and Saito, E., 1971. Deuterium isotope effect on the decay kinetics of perhydroxyl radical, J. Phys. Chem. 75: 2263–2266.
Bors, W., Saran, M., Longfelder, E., Michel, C., Fuchs, C., and Frenzel, C., 1978. Detection of oxygen radicals in biological systems, Photochem. Photobiol. 28: 629–638.
Bors, W., Michel, C., and Saran, M., 1979. Superoxide anions do not react with hydroperoxides, FEBS Lett. 107: 403–406.
Britton, L., Malinouski, D. P., and Fridovich, 1., 1978. Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms, J. Bacteriol. 134: 229–236.
Chern, C.-I., and San Filippo, J., 1977. The reaction of superoxide with hydrazines, hydrazones, and related compounds, J. Org. Chem. 42: 178–180.
Corey, E. J., Nicolaou, K. C., Shibasaki, M., Machida, Y., and Shiner, C. S., 1975. Superoxide ion as a synthetically useful oxygen nucleophile, Tetrahedron Lett. 1975: 3183–3186.
Czapski, G., 1978, Photochem. Photobiol. 28:926 (in the Discussion).
Czapski, G., and Ilan, Y. A., 1978. On the generation of the hydroxylation agent from superoxide radical: Can the Haber-Weiss reaction be the source of OH radicals?, Photochem. Photobiol. 28: 651–653.
Danen, W. D. and Arudi, R. L., 1978. Generation of singlet oxygen in the reaction of superoxide anion radical with diacyl peroxides, J. Am. Chem. Soc. 100: 3944–3945.
Danen, W. C., and Warner, R. J., 1977. The remarkable nucleophilicity of superoxide anion radical: Rate constants for reactions of superoxide with aliphatic bromides, Tetrahedron Lett. 1977: 989–992.
Darnall, K., Winer, A. M., Lloyd, A. C., and Pitts, J. N., Jr., 1976. Relative rate constants for the reaction of OH radicals with selected C6 and C7 alkanes and alkenes at 305 ± 2°K, Chem. Phys. Lett. 44: 415–418.
Darnall, K. R., Atkinson, R., and Pitts, J. N., Jr., 1978. Rate constants for the reaction of the OH radical with selected alkanes at 300°K, J. Phys. Chem. 82: 1581–1584.
Fee, J. A., 1980. A comment on the hypothesis that oxygen toxicity is mediated by superoxide, in Oxygen and Life, Burlington House, London, Royal Society of London, pp. 77–97.
Fee, J. A., and Hildebrand, P. G., 1974. On the development of a well-defined source of superoxide ion for studies with biological studies, FEBS Lett. 39: 79–82.
Ferradini, C., Foos, J., Houee, C., and Pauchault, J., 1978. The reaction between superoxide anion and hydrogen peroxide, Photochem. Photobiol. 28: 697–700.
Fielden, E. M., Cohen, G., Bors, W., and Czapski, G., 1978. Photochem. Photobiol. 28:674–675 (in the Discussion).
Finkelstein, E., Rosen, G. M., and Rauchman, E. J., 1980. Spin trapping of superoxide and hydroxyl radical: Practical aspects, Arch. Biochem. Biophys. 200: 1–6.
Foote, C. S., 1978. Untitled paper, Photochem. Photobiol. 28: 718–740.
Foote, C. S., Shook, F. C., and Abakerli, R. A., 1980a. Chemistry of superoxide ion. 4. Singlet oxygen is not a major product of dismutation, J. Am. Chem. Soc. 102: 2503–2504.
Foote, C. S., Abakerli, R. B., Clough, R. L., and Shook, F. C., 1980b. On the question of singlet oxygen production in leucocytes, macrophages, and the dismutation of superoxide anion, in Biological and Clinical Aspects of Superoxide and Superoxide Dismutase, W. H. Bannister and
J. V. Bannister (eds.), Proceedings of the Federation of European Biochemical Societies Symposium No. 62, Elsevier, New York, pp. 222–230.
Fridovich, I., 1974. Superoxide dismutase, Adv. Enzymol. 41: 35–97.
Fridovich, I., 1978a. The biology of oxygen radicals, Science 201: 875–880.
Fridovich, I., 1978b. Superoxide radicals, superoxide dismutases, and the aerobic lifestyle, Photochem. Photobiol. 28: 733–740.
Frimer, A. A., and Rosenthal, 1., 1978. Chemical reactions of superoxide anion radical in aprotic solvents, Photochem. Photobiol. 28: 711–719 (and Discussion following).
Frimer, A. A., Rosenthal, I., and Hoz, S., 1977. The reaction of superoxide anion radical with electron poor olefins, Tetrahedron Lett. 1977: 4631–4634.
Gibian, M. J., and Ungermann, T., 1976. Reaction of tert-butyl hydroperoxide anion with dimethyl sulfoxide: On the pathway of the superoxide-alkyl halide reaction, J. Org. Chem. 41: 2500–2502.
Gregory, E. M., Yost, F. J., Jr., and Fridovich, I., 1973. Superoxide dismutases of Escherichia coli: Intracellular localizations and functions, J. Bacteriol. 115: 987–991.
Guiraud, H. J., and Foote, C. S., 1976. Chemistry of superoxide ion. III. Quenching of singlet oxygen, J. Am. Chem. Soc. 98: 1984–1986.
Haber, F., and Weiss, J., 1934. The catalytic decomposition of hydrogen peroxide by iron salts, Proc. R. Soc. London Ser. A 147: 332–351.
Heicklen, J., 1981. The correlation of rate coefficients for H-atom abstraction by HO radicals with C-H bond dissociation enthalpies, Int. J. Chem. Kinet. 13: 651–665.
Hiller, K. O., Mastoch, B., Gobt, M., and Asmus, L. D., 1981. Mechanism of OH radical induced oxidation of methionine in aqueous solution, J. Am. Chem. Soc. 103: 2734–2743.
Hirata, F., and Hayaishi, O., 1975. Studies on indoleamine 2,3-dioxygenase. I. Superoxide anion as substrate, J. Biol. Chem. 250: 5960–5966.
Hodgson, E. K., and Fridovich, I., 1973. Reversal of the superoxide dismutase reaction, Biochem. Biophys. Res. Commun. 54: 270–274.
House, H. O., 1972. Modern Synthetic Reactions, Benjamin/Cummings, Menlo Park, California, pp. 307–312.
Howard, D. J., 1980. Kinetic study of the equilibrium HO2 + NO;:± OH + NO2 and the thermochemistry of HO2, J. Am. Chem. Soc. 102: 6937–6941.
Ilan, Y. A., Meisel, D., and Czapski, G., 1974. The redox potential of the O2-O2 system in aqueous media, Isr. J. Chem. 12: 891–895.
Jeong, K.-M., and Kaufman, F., 1982. Kinetics of the reaction of hydroxyl radical with methane and with nine Cl- and F-substituted methanes. 2. Calculation of rate parameters as a test of transition state theory, J. Phys. Chem. 88: 1816–1821.
Johnson, R. A., and Nidy, E. G., 1975. Superoxide chemistry: A convenient synthesis of dialkyl peroxides, J. Org. Chem. 40: 1680–1681.
Keele, B. B., Jr., McCord, J. M., and Fridovich, I., 1970. Superoxide dismustase from Escherichia coli B, J. Biol. Chem. 245: 6176–6181.
Khan, A. U., 1978. Activated oxygen: Singlet molecular oxygen and superoxide anion, Photochem. Photobiol. 28: 615–626 (and Dicussion following).
Klug-Roth, D., Fridovich, I., and Rabani, J., 1973. Pulse radiolytic investigations of superoxide catalyzed disproportionation: Mechanism for bovine superoxide dismutase, J. Am. Chem. Soc. 95: 2786–2790.
Kobayashi, S., and Ando, W., 1979. Co-oxidation of 1, 3-diphenylisobenzofuran by the Haber-Weiss reaction: Is singlet oxygen concerned in this reaction?, Biochem. Biophys. Res. Commun. 188: 676–681.
Koppenol, W. H., and Butler, J., 1977. Mechanism of reactions involving singlet oxygen and the superoxide anion, FEBS Lett. 83: 1–6.
Koppenol, W. H., Butler, J., and vanLeeuwen, J. W., 1978. The Haber-Weiss cycle, Biochem. Biophys. Res. Commun. 188: 655–658 (and Discussion following).
Lavelle, F., McAdam, M. E., Fielden, E. M., Roberts, P. B., Puget, K., and Michelson, A. M., 1977. A pulse-radiolytis study of the catalytic mechanism of the iron-containing superoxide dismutase from Photobacterium leiognathi, Biochem. J. 161: 2–11.
Lee-Ruff, E., 1977. The organic chemistry of superoxide, Chem. Soc. Rev. 6: 195–214.
Lieberman, R. A., and Fee, J. A., 1973. Preliminary report on the electron paramagnetic resonance spectra of singlet crystals of bovine erythrocyte superoxide dismutase, J. Biol. Chem. 248: 7617–7619.
Liotta, C. L., and Harris, H. P., 1974. The chemistry of “naked” anions. I. Reactions of the 18crown-6 complex of potassium fluoride with organic substrates in aprotic solvents, J. Am. Chem. Soc. 96: 2250–2252.
Marklund, S., 1976. Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase, J. Biol. Chem. 251: 7504–7507.
Matsumoto, S., and Matsuo, M., 1977. The reaction of a a-tocopherol model compound with K02, a new oxidation product of 6-hydroxy-2,2,5,7,8-penta-methylchroman, Tetrahedron Lett. 1977: 1999–2000.
May, S. W., Abbott, B. J., and Felix, A., 1973. On the role of superoxide in reactions catalyzed by rubredoxin of Pseudomonas oleovorans, Biochem. Biophys. Res. Commun. 54:1540–1545. Mayer, R., Widom, J., and Que, Jr., L., 1980, Involvement of superoxide in the reactions of the catechol dioxygenases, Biochem. Biophys. Res. Commun. 92: 285–291.
McCandish, E., Miksztal, A. R., Nappa, M., Springer, A. Q., Valentine, J. S., Stong, J. D., and Spiro, T. G., 1980. Reactions of superoxide with iron porphyrins in aprotic solvents: A high spin ferric porphyrin peroxo complex, J. Am. Chem. Soc. 102: 4268–4271.
McCord, J. M., and Day, E. D., 1978. Superoxide dependent production of hydroxyl radical catalyzed by iron-EDTA complex, FEBS Lett. 86: 139–142.
McCord, J. M., and Fridovich, 1., 1968. The reduction of cytochrome c by milk xanthine oxidase, J. Biol. Chem. 243: 5753–5760.
McElroy, A. D., and Hashman, J. S., 1964. Synthesis of tetramethylammonium superoxide, Inorg. Chem. 3: 1798–1799.
McIsaac, J. E., Subbaraman, L. R., Subbaraman, J., Mulhausen, H. A., and Behrman, E. J., 1972. The nucleophilic reactivity of peroxy anions, J. Org. Chem. 37: 1037–1041.
Merritt, M. V., and Johnson, R. A., 1977. Spin trapping, alkylperoxy radicals, and superoxide-alkyl halide reactions, J. Am. Chem. Soc. 99: 3713–3719.
Merritt, H., and Sawyer, D. T., 1970. Electrochemical studies of the reactivity of superoxide ion with several alkyl halides in dimethyl sulfoxide, J. Org. Chem. 35: 2157–2159.
Milligan, D. E., and Jacox, M. E., 1963. Infrared spectroscopic evidence for the species HO2, J. Chem. Phys. 38: 2627–2631.
Misra, H., and Fridovich, I., 1972a. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismustase, J. Biol. Chem. 247: 3170–3175.
Misra, H., and Fridovich, I., 1972b. The generation of superoxide radical during the autoxidation of hemoglobin, J. Biol. Chem. 247: 6960–6962.
Moro-Oka, Y., and Foote, C. S., 1976. Chemistry of superoxide ion. I. Oxidation of 3,5-di-tertbutylcatechol with KO2, J. Am. Chem. Soc. 98: 1510–1514.
Nilsson, R. and Kearns, D. R., 1974. Some useful heterogeneous systems for photosensitized generation of singlet oxygen, Photochem and Photobiol. 19: 181–184.
Ose, D. E., and Fridovich, I. 1979. A manganese-containing superoxide dismutase from Escherichia coli: A reversible resolution and metal replacements, Arch. Biochem. Biophys: 194: 360–364.
Overend, R., and Paraskevopoulos, G., 1978. Rates of OH radical reaction. 4. Reactions with methanol, ethanol, 1-propanol, and 2-propanol at 296°K, J. Phys. Chem. 82: 1329–1333.
Ozawa, T., Hanaki, A., and Yamamoto, H. 1977. On a spectrally well-defined and stable source of superoxide ion, O2, FEBS Lett. 74: 99–102.
Paraskevopoulos, G., and Nip, W. S., 1980. Rates of OH radical reactions. VII. Reactions of OH and OD radicals with n-C4H,o, n-C4D,o, H2 and D2, and of OH with n-C5H,2 at 297°K, Can. J. Chem. 58: 2146–2149.
Pedersen, C. J., 1967. Cyclic polyethers and their complexes with metal salts, J. Am. Chem. Soc. 89: 7017–7036.
Peters, J. W., and Foote, C. S., 1976. Chemistry of superoxide ion. II. Reaction with hydroperoxides, J. Am. Chem. Soc. 98: 873–875.
Pick, M., Rabani, J., Yost, F., and Fridovich, I., 1974. The catalytic mechanism of the manganesecontaining superoxide dismutase of Escherichia coli studied by pulse radiolysis, J. Am. Chem. Soc. 96: 7329–7333.
Poupko, R., and Rosenthal, I., 1973. Electron transfer interactions between superoxide ion and organic compounds, J. Chem. Phys. 77: 1722–1724.
Pryor, W. A., and Tang, R. H., 1978. Ethylene formation from methional, Biochem. Biophys. Res. Commun. 81: 498–503.
Rabani, J., and Nielsen, S. 0., 1969. Absorption spectrum and decay kinetics of 02 and H02 in aqueous solutions by pulse radiolysis, J. Phys. Chem. 73: 3736–3744.
Reichelt, J. L., Nealson, K., and Hastings, J. W., 1977. The specificity of symbiosis: Pony fish and luminescent bacteria, Arch. Microbiol. 112: 157–161.
Richardson, J. S., Thomas, K. A., Rubin, B. H., and Richards, D. C., 1975. Crystal structure of bovine Cu, Zn in superoxide dismutase at 3 A resolution: Chain tracing and metal ligands, Proc. Nad. Acad. Sci. U.S.A. 72: 1349–1353.
Roberts, J. L., Jr., and Sawyer, D. T., 1981. Facile degradation by superoxide ion of carbon tetrachloride, chloroform, methylene chloride and p,p-DDT in aprotic media, J. Am. Chem. Soc. 103: 712–714.
Rotilio, G., Finazzi-Agro, A., Calabrese, L., Bossa, F., Guerrieri, P., and Mondovi, B., 1971. Studies of the metal sites of copper proteins, ligands of copper in hemocuprein, Biochemistry 10: 616–621.
Rotilio, G., Bray, R. C., and Fielden, E. M., 1972a. A pulse radiolysis study of superoxide dismutase, Biochim. Biophys. Acta 286: 605–609.
Rotilio, G., Calabrese, L., Bossa, F., Barra, D., Finazzi-Agro, A., and Mondovi, B., 1972b. Properties of the apo-protein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase, Biochemistry, 11: 2182–2187.
Rotilio, G., Morpurgo, L., Gioviagnoli, C., Calabrese, L., and Mondovi, B., 1972c. Studies of the metal sites of copper proteins: Symmetry of copper in bovine superoxide dismutase and its functional significance, Biochemistry 11: 2187–2192.
Rotilio, G., Morpurgo, L., Calabresse, L., and Mondovi, B., 1973. On the mechanism of superoxide dismutase reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide, Biochim. Biophys. Acta 302: 229–235.
Sagae, H., Fujihira, M., Osa, T., and Lund, H., 1977. Oxidation of nitroalkylbenzene with electrogenerated superoxide ion, Chem. Soc. Jpn. Chem. Lett. 1977: 793–796.
Sagae, H., Fujihira, M., Lund, H., and Osa, T., 1980. Oxidation of nitrotoluenes with electrogenerated superoxide ion, Bull. Chem. Soc. Jpn. 53: 1537–1541.
Saito, I., Otsuki, T., and Matsuura, T., 1979. The reaction of superoxide ion with vitamin K1 and its related compounds, Tetrahedron Lett. 1979: 1693–1696.
San Filippo, J., and Chern, C.-I., 1976. Oxidative cleavage of a-keto, a-hydroxy, and a-halo ketones, esters, and carboxylic acids by superoxide, J. Org. Chem. 41: 1077–1078.
San Filippo, J., Romano, L. J., Chern, C.-I., and Valentine, J. S., 1976. Cleavage of esters by superoxide, J. Org. Chem. 41: 586–588.
Sanka, J., and Martinsons, V., 1968. Chemical properties of potassium peroxide, Chem. Abstr. 68: 45846A.
Sawyer, D. T., and Gibian, M. J., 1979. The chemistry of superoxide ion, Tetrahedron 35: 1471–1481.
Sawyer, D. T., and Valentine, J. S., 1981. How super is superoxide?. Acc. Chem. Res. 14: 393–399.
Sawyer, D. T., Gibian, M. J., Morrison, M. M., and Seo, E. T., 1978. On the chemical reactivity of superoxide ion, J. Am. Chem. Soc. 100: 627–628.
Scully, F. E., Jr., and Davis, R. C., 1978. Superoxide in organic synthesis: A new mild method for the oxidation of amines to carbonyls via N-chloroamines, J. Org. Chem. 43: 1467–1468.
Seyb, E., and Kleinberg, J., 1951. Determination of superoxide oxygen, Anal. Chem. 23: 115–117.
Stanley, J. P., 1980. Reactions of superoxide with peroxides, J. Org. Chem. 45:1413–1418. Steinman, H. M., and Hill, R. L., 1973. Sequence homologies among bacterial and mitochondrial superoxide dismutases, Proc. Natl. Acad. Sci. U.S.A. 70: 3725–3729.
Steinman, H. M., Vishweshwar, R. N., Abernethy, J. L., and Hill, R. L., 1974. Bovine erythrocyte superoxide dismutase: Complete amino acid sequence, J. Biol. Chem. 249: 7326–7338.
Tezuka, M., Ohkatsu, Y., and Osa, T., 1975. Reactivity of electrogenerated superoxide ion. I. Autoxidation of 9,10-dihydroanthracene, Bull. Chem. Soc. Jpn. 48: 1471–1474.
Thomas, K. A., Rubin, B. H., Bier, J. C., Richardson, J. S., and Richardson, D. C., 1974. The crystal structure of bovine Cu,, Zn2 + superoxide dismutase at 5.5 A resolution, J. Biol. Chem. 249: 5677–5683.
Thomas, M. J., Mehl, K. S., and Pryor, W. A., 1978. The role of superoxide anion in the xanthine oxidase-induced autoxidation of linoleic acid, Biochem. Biophys. Res. Commun. 83: 927–932.
Valentine, J. S., and Curtis, A. B., 1975. A convenient preparation of solutions of superoxide anion and the reaction of superoxide anion with a copper(II) complex, J. Am. Chem. Soc. 97: 224–226.
Vance, D. G., Keele, B. B., Jr., and Rajagopalan, K. V., 1972. Superoxide dismutase from Streptococcus mutans, J. Biol. Chem. 247: 4782–4786.
Varney, R. N., Pahl, M., and Mark, T. D., 1973. Properties of the ionic system N4+ -, 04+ -, and 04 -, Acta Phys. Austriaca 38: 287–294.
Wallace, M. J., Maxwell, J. C., and Caughey, W. S., 1974. The mechanisms of hemoglobin autoxidation: Evidence for proton-assisted nucleophilic displacement of superoxide by anions, Biochem. Biophys. Res. Commun. 57: 1104–1110.
Weinstein, J., and Bielski, B. H. J., 1979. Kinetics of the interaction of HO2 and O2 radicals with hydrogen peroxide: The Haber-Weiss reaction, J. Am. Chem. Soc. 101: 58–62.
Weisiger, R. A., and Fridovich, I., 1973. Superoxide dismutase, J. Biol. Chem. 248:3582–3592. Weser, U., Bunnenberg, E., Cammack, R., Djerassi, C., Flohe, L., Thomas, G., and Voelter, W., 1971. A study on purified bovine erythrocuprein, Biochim, Biophys, Acta 243;203–213.
Wever, R., Oudega, B., and Van Gelder, B. F., 1973. Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin, Biochim. Biophys. Acta 302: 475–478.
Wilshire, J., and Sawyer, D. T., 1979. Redox chemistry of dioxygen species, Acc. Chem. Res. 12: 105–110.
Yost, F. J. and Fridovich,I., 1973. An iron containing superoxide dismutase from Escherichia coli, J. Biol. Chem. 248: 4905–4908.
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Ingraham, L.L., Meyer, D.L. (1985). Superoxide Ion. In: Biochemistry of Dioxygen. Biochemistry of the Elements, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2475-1_4
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