Superoxide radical and superoxide dismutases

Fridovich, Irwin

doi:10.1146/annurev.bi.64.070195.000525

Cited by 3,455Redox biology and oxidative stressMetal-Catalyzed Oxygenation MechanismsGlutathione Transferases and Polymorphisms

Superoxide radical and superoxide dismutases

Fridovich, Irwin·1995·Annual Review of Biochemistry

DOI 10.1146/annurev.bi.64.070195.000525

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Abstract

O2- oxidizes the [4Fe-4S] clusters of dehydratases, such as aconitase, causing-inactivation and release of Fe(II), which may then reduce H2O2 to OH- +OH.. SODs inhibit such HO. production by scavengingO2-, but Cu, ZnSODs, by virtue of a nonspecific peroxidase activity, may peroxidize spin trapping agents and thus give the appearance of catalyzing OH. production from H2O2. There is a glycosylated, tetrameric Cu, ZnSOD in the extracellular space that binds to acidic glycosamino-glycans. It minimizes the reaction of O2- with NO. E. coli, and other gram negative microorganisms, contain a periplasmic Cu, ZnSOD that may serve to protect against extracellular O2-. Mn(III) complexes of multidentate macrocyclic nitrogenous ligands catalyze the dismutation of O2- and are being explored as potential pharmaceutical agents. SOD-null mutants have been prepared to reveal the biological effects of O2-. SodA, sodB E. coli exhibit dioxygen-dependent auxotrophies and enhanced mutagenesis, reflecting O2(-)-sensitive biosynthetic pathways and DNA damage. Yeast, lacking either Cu, ZnSOD or MnSOD, are oxygen intolerant, and the double mutant was hypermutable and defective in sporulation and exhibited requirements for methionine and lysine. A Cu, ZnSOD-null Drosophila exhibited a shortened lifespan.

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MnSOD is most abundant in the mitochondria, whereas Cu,Zn-SOD predominates in the cytoplasm.
“MnSOD is most abundant in the mitochondria, whereas Cn, Zn-SOD predominates in the cytoplasm [11].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [11]
Mammalian cells contain three forms of SOD: Mn-SOD, cytosolic Cu,Zn-SOD and extracellular Cu,Zn-SOD.
“Mammalian cells contain three forms of SOD: Mn-SOD, cytosolic Cu, Zn-SOD and extracellular Cu, Zn-SOD.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [11]
In some assays, O2 reduces tetranitro methane, cytochrome c or nitro tetrazolium blue, and in others it oxidises epinephrine, tiron pyrogallol or 6-hydroxydopamine.
“Thus, in some assays, Oz reduces tetranitro methane [11], cytochrome c or nitro tetrazolium blue [100], and in others it oxidises epinephrine, tiron pyrogallol or 6-hydroxydopamine [101,102], Figure 38.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [11]

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Subcellular Location of Superoxide Dismutase in Spinach Leaves and Preparation and Properties of Crystalline Spinach Superoxide Dismutase
Asada, K., Urano, M., & Takahashi, M. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02908.x · Cited by 182 · see citing works
Reversal of the superoxide dismutase reaction
Hodgson, E. K., & Fridovich, I. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90918-2 · Cited by 180 · see citing works
Self-citation
p-Nitrosodimethylaniline as an OH Radical Scavenger in Radiation Chemistry1
Kraljić, I., & Trumbore, C. N. (1965) · Journal of the American Chemical Society · doi:10.1021/ja01090a004 · Cited by 180 · see citing works
THE EFFECT OF IRON ON THE DISTRIBUTION OF SUPEROXIDE AND HYDROXYL RADICALS AS SEEN BY SPIN TRAPPING AND ON THE SUPEROXIDE DISMUTASE ASSAY
Buettner, G. R., Oberley, L. W., & Leuthauser, S. W. C. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07001.x · Cited by 179 · see citing works
Superoxide formation in spinach chloroplasts: Electron spin resonance detection by spin trapping
Harbour, J. R., & Bolton, J. R. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(75)90118-7 · Cited by 178 · see citing works
Developmental Characteristics of Pulmonary Superoxide Dismutase: Relationship to Idiopathic Respiratory Distress Syndrome
Autor, A. P., Frank, L., & Roberts, R. J. (1976) · Pediatric Research · doi:10.1203/00006450-197603000-00002 · Cited by 178 · see citing works
Biological protection by superoxide dismutase
Lavelle, F., Michelson, A. M., & Dimitrijevic, L. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)91094-2 · Cited by 173 · see citing works
One-electron reactions in biochemical systems as studied by pulse radiolysis
Land, E. J., & Swallow, A. J. (1971) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(71)90049-x · Cited by 171 · see citing works
Superoxide Dismutase and Oxygen Toxicity in a Eukaryote
Gregory, E. M., Goscin, S. A., & Fridovich, I. (1974) · Journal of Bacteriology · doi:10.1128/jb.117.2.456-460.1974 · Cited by 168 · see citing works
Self-citation
Studies related to antitumor antibiotics. Part V. Reactions of mitomycin C with DNA examined by ethidium fluorescence assay
Lown, J. W., Begleiter, A., Johnson, D. S., & Morgan, A. R. (1976) · Canadian Journal of Biochemistry · doi:10.1139/o76-018 · Cited by 168 · see citing works
Isolation of a new copper — Containing superoxide dismutase bacteriocuprein
Puget, K., & Michelson, A. M. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80492-4 · Cited by 167 · see citing works
Superoxide Dismutases of Escherichia coli : Intracellular Localization and Functions
Gregory, E. M., Yost, F. J., & Fridovich, I. (1973) · Journal of Bacteriology · doi:10.1128/jb.115.3.987-991.1973 · Cited by 166 · see citing works
Self-citation
The Pulse Radiolysis of Aqueous Tetranitromethane.1 I. Rate Constants and the Extinction Coefficient of eaq-. II. Oxygenated Solutions
Rabani, J., Mulac, W. A., & Matheson, M. S. (1965) · The Journal of Physical Chemistry · doi:10.1021/j100885a011 · Cited by 166 · see citing works
THE ROLE OF SUPEROXIDE AND SINGLET OXYGEN IN LIPID PEROXIDATION
Svingen, B. A., O'Neal, F. O., & Aust, S. D. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07022.x · Cited by 166 · see citing works
The oxidation of tiron by superoxide anion. Kinetics of the reaction in aqueous solution and in chloroplasts
Greenstock, C. L., & Miller, R. W. (1975) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(75)90184-x · Cited by 157 · see citing works
Ethylene formation from methional
Pryor, W. A., & Tang, R. H. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91562-0 · Cited by 156 · see citing works
Polarographic determination of superoxide dismutase
Rigo, A., Viglino, P., & Rotilio, G. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90672-7 · Cited by 155 · see citing works
Superoxide Dismutase and Oxygen Metabolism inStreptococcus faecalisand Comparisons with Other Organisms
Britton, L. N., Malinowski, D. P., & Fridovich, I. (1978) · Journal of Bacteriology · doi:10.1128/jb.134.1.229-236.1978 · Cited by 154 · see citing works
Self-citation
Inhibition of superoxide dismutases by azide
Misra, H. P., & Fridovich, I. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90218-7 · Cited by 154 · see citing works
Self-citation
Ethylene production from methionine
Lieberman, M., Kunishi, A. T., Mapson, L. W., & Wardale, D. A. (1965) · Biochemical Journal · doi:10.1042/bj0970449 · Cited by 151 · see citing works
Superoxide dismutase in anaerobic bacteria of clinical significance
Tally, F. P., Goldin, B. R., Jacobus, N. V., et al. (1977) · Infection and Immunity · doi:10.1128/iai.16.1.20-25.1977 · Cited by 148 · see citing works
The sites of superoxide anion generation in higher plant mitochondria
Rich, P. R., & Bonner, W. D. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90373-9 · Cited by 146 · see citing works
The spectrophotometry of dense light-scattering material
Butler, W. L., & Norris, K. H. (1960) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(60)90119-3 · Cited by 146 · see citing works
Mechanisms of Oxidation with Oxygen
Taube, H. (1965) · The Journal of General Physiology · doi:10.1085/jgp.49.1.29 · Cited by 145 · see citing works
Superoxide Dismutase from Streptococcus mutans
Vance, P. G., Keele, B. B., & Rajagopalan, K. V. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44979-x · Cited by 142 · see citing works
Characterization of Enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system.
Mieyal, J. J., Ackerman, R., Blumer, J. L., et al. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33457-9 · Cited by 139 · see citing works
Superoxide dismutase and the oxygen enhancement of radiation lethality
Misra, H. P., & Fridovich, I. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90201-0 · Cited by 139 · see citing works
Self-citation
A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine
Heikkila, R. E., & Cabbat, F. S. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90089-0 · Cited by 138 · see citing works
Studies on indoleamine 2,3-dioxygenase. I. Superoxide anion as substrate.
Hirata, F., & Hayaishi, O. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41144-7 · Cited by 138 · see citing works
The mechanism of the oxidation of ascorbate and Mn2+ by chloroplasts: The role of the radical superoxide
Epel, B. L., & Neumann, J. (1973) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(73)90211-9 · Cited by 133 · see citing works
The Purification and Properties of Superoxide Dismutase from Neurospora crassa
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45155-7 · Cited by 132 · see citing works
Self-citation
Iron containing superoxide dismutases from luminous bacteria
Puget, K., & Michelson, A. M. (1974) · Biochimie · doi:10.1016/s0300-9084(74)80019-2 · Cited by 131 · see citing works
Formation of Superoxide in the Autoxidation of the Isolated alpha and beta Chains of Human Hemoglobin and Its Involvement in Hemichrome Precipitation
Brunori, M., Falcioni, G., Fioretti, E., Giardina, B., & Rotilio, G. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb04046.x · Cited by 130 · see citing works
Radioprotective effect of superoxide dismutase on model phospholipid membranes
Petkau, A., & Chelack, W. S. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90272-8 · Cited by 129 · see citing works
Superoxide dismutase in some obligately anaerobic bacteria
Hewitt, J. A. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80518-7 · Cited by 127 · see citing works
The kinetics of the reduction of cytochrome c by the superoxide anion radical
Koppenol, W. H., Buuren, K. J. H. V., Butler, J., & Braams, R. (1976) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(76)90130-4 · Cited by 126 · see citing works
THE FORMATION AND DECAY OF H2O3 AND HO2 IN ELECTRON-IRRADIATED AQUEOUS SOLUTIONS1
Czapski, G., & Bielski, B. H. J. (1963) · The Journal of Physical Chemistry · doi:10.1021/j100804a050 · Cited by 126 · see citing works
Spin trapping and its application in the study of lipid peroxidation and free radical production with liver microsomes
Saprin, A. N., & Piette, L. H. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90063-7 · Cited by 125 · see citing works
Catalytic mechanism of the manganese-containing superoxide dismutase of Escherichia coli studied by pulse radiolysis
Pick, M. R., Rabani, J., Yost, F., & Fridovich, I. (1974) · Journal of the American Chemical Society · doi:10.1021/ja00830a026 · Cited by 124 · see citing works
Self-citation
A pulse-radiolysis study of the manganese-containing superoxide dismutase from Bacillus stearothermophilus. A kinetic model for the enzyme action
McAdam, M. E., Fox, R. A., Lavelle, F., & Fielden, E. M. (1977) · Biochemical Journal · doi:10.1042/bj1650071 · Cited by 123 · see citing works
Generation of hydrogen peroxide, superoxide and hydroxyl radicals during the oxidation of dihydroxyfumaric acid by peroxidase
Halliwell, B. B. (1977) · Biochemical Journal · doi:10.1042/bj1630441 · Cited by 122 · see citing works
The mechanism of the activity-dependent luminescence of xanthine oxidase
Hodgson, E. K., & Fridovich, I. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90067-9 · Cited by 122 · see citing works
Self-citation
Ethylene formation by polymorphonuclear leukocytes. Role of myeloperoxidase.
Klebanoff, S. J., & Rosen, H. (1978) · The Journal of Experimental Medicine · doi:10.1084/jem.148.2.490 · Cited by 122 · see citing works
The mechanism of DNA strand breakage by vitamin C and superoxide and the protective roles of catalase and superoxide dismutase
Morgan, A. R., Cone, R. L., & Terry, M. E. (1976) · Nucleic Acids Research · doi:10.1093/nar/3.5.1139 · Cited by 121 · see citing works
THE ROLE OF O2‐ IN THE CHEMILUMINESCENCE OF LUMINOL*
Hodgson, E. K., & Fridovich, I. (1973) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1973.tb06449.x · Cited by 120 · see citing works
Self-citation
REACTIONS OF O‐2, H2O2 AND OTHER OXIDANTS WITH SULFHYDRYL ENZYMES‡
Armstrong, D. A., & Buchanan, J. D. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07011.x · Cited by 120 · see citing works
ON THE GENERATION OF THE HYDROXYLATION AGENT FROM SUPEROXIDE RADICAL. CAN THE HABER–WEISS REACTION BE THE SOURCE OF OH RADICALS?
Czapski, G., & Ilan, Y. A. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb06988.x · Cited by 119 · see citing works
Stopped flow spectrophotometric observation of superoxide dismutation in aqueous solution
McClune, G. J., & Fee, J. A. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80550-9 · Cited by 119 · see citing works
Inactivation of biologically active DNA by γ-ray-induced superoxide radicals and their dismutation products singlet molecular oxygen and hydrogen peroxide
HEMMEN, J. J. V., & Meuling, W. J. A. (1975) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(75)90031-3 · Cited by 117 · see citing works
Kinetics of the Decomposition of Hydrogen Peroxide Catalyzed by Ferric Ethylenediaminetetraacetate Complex
Walling, C. T., Partch, R. E., & Weil, T. M. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.140 · Cited by 116 · see citing works
An attempt to demonstrate a reaction between superoxide and hydrogen peroxide
Halliwell, B. B. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80801-0 · Cited by 116 · see citing works
Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid
Forman, H. J., & Kennedy, J. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41421-x · Cited by 115 · see citing works
Radioprotection of mice by superoxide dismtuase
Petkau, A., Chelack, W. S., Pleskach, S. D., Meeker, B. E., & Brady, C. M. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(75)80468-2 · Cited by 115 · see citing works
Oxidation-reduction properties of bovine erythrocyte superoxide dismutase
Fee, J. A., & DiCorleto, P. E. (1973) · Biochemistry · doi:10.1021/bi00748a013 · Cited by 111 · see citing works
Bovine Erythrocyte Superoxide Dismutase
Abernethy, J. L., Steinman, H. M., & Hill, R. L. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42109-1 · Cited by 110 · see citing works
The amino acid sequence of mangano superoxide dismutase from Escherichia coli B.
Steinman, H. M. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34235-7 · Cited by 110 · see citing works
Oxygen Metabolism in Lactobacillus plantarum
Gregory, E. M., & Fridovich, I. (1974) · Journal of Bacteriology · doi:10.1128/jb.117.1.166-169.1974 · Cited by 109 · see citing works
Self-citation
Inhibition of superoxide anion production in macrophages by anti-inflammatory drugs
Ōyanagui, Y. (1976) · Biochemical Pharmacology · doi:10.1016/0006-2952(76)90063-0 · Cited by 108 · see citing works
The purification and properties of superoxide dismutase from Saccharomyces cerevisiae
Goscin, S. A., & Fridovich, I. (1972) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(72)90078-2 · Cited by 107 · see citing works
Self-citation
Generation of the Superoxide Radical during Autoxidation of Oxymyoglobin
Gotoh, T., & Shikama, K. (1976) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131289 · Cited by 107 · see citing works
On the formation of the superoxide anion radical during the reaction of reduced iron-sulfur proteins with oxygen
Orme‐Johnson, W. H., & Beinert, H. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90289-7 · Cited by 105 · see citing works
Sequence Homologies Among Bacterial and Mitochondrial Superoxide Dismutases
Steinman, H. M., & Hill, R. L. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.12.3725 · Cited by 103 · see citing works
Effects of superoxide radicals on myoblast growth and differentiation
Michelson, A. M., & BUCKINGHAM, M. E. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80254-8 · Cited by 100 · see citing works
Superoxide Dismutase in the Anaerobic Flagellates, Tritrichomonas foetus and Monocercomonas sp
Lindmark, D. G., & Müller, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42465-4 · Cited by 99 · see citing works
Oxidation of manganous pyrophosphate by superoxide radicals and illuminated spinach chloroplasts
Kono, Y., Takahashi, M., & Asada, K. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90373-8 · Cited by 97 · see citing works
Free radical reduction of ferricytochrome-c
Simic, M. G., Taub, I. A., Tocci, J., et al. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(75)80118-5 · Cited by 97 · see citing works
Superoxide Dismutase from Mycobacterium tuberculosis
Kusunose, E., Ichihara, K., Yojiro, N. O. D. A., et al. (1976) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131407 · Cited by 97 · see citing works
Inhibition by superoxide dismutase of methemoglobin formation from oxyhemoglobin.
Lynch, R. E., Lee, R., & Cartwright, G. E. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33794-8 · Cited by 96 · see citing works
An attempt to evaluate the rate of the haber‐weiss reaction by using ·OH radical scavengers
Rigo, A., Stevanato, R., Finazzi‐Agrò, A., & Rotilio, G. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80422-5 · Cited by 96 · see citing works
Superoxide Radical as an Intermediate in the Oxidation of Hydroxylamines by Mixed Function Amine Oxidase
Rauckman, E. J., Rosen, G. M., & Kitchell, B. B. (1979) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)11537-x · Cited by 95 · see citing works
A pulse-radiolysis study of the catalytic mechanism of the iron-containing superoxide dismutase from Photobacterium leiognathi
Lavelle, F., McAdam, M. E., Fielden, E. M., Roberts, P. B., Puget, K., & Michelson, M. (1977) · Biochemical Journal · doi:10.1042/bj1610003 · Cited by 94 · see citing works
Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex.
Hirata, F., Ohnishi, T., & Hayaishi, O. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40208-0 · Cited by 94 · see citing works
The role of the superoxide anion in the xanthine oxidase-induced autoxidation of linoleic acid
Thomas, M. J., Mehl, K. S., & Pryor, W. A. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91484-5 · Cited by 92 · see citing works
Regulation of superoxide dismutase synthesis in Escherichia coli: glucose effect
Hassan, H. M., & Fridovich, I. (1977) · Journal of Bacteriology · doi:10.1128/jb.132.2.505-510.1977 · Cited by 92 · see citing works
Self-citation
Effect of diethyldithiocarbamate on oxygen toxicity and lung enzyme activity in immature and adult rats
Frank, L., Wood, D. L., & Roberts, R. J. (1978) · Biochemical Pharmacology · doi:10.1016/0006-2952(78)90311-8 · Cited by 92 · see citing works
Superoxide dismutase and peroxidase: A positive activity stain applicable to polyacrylamide gel electropherograms
Misra, H. P., & Fridovich, I. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90386-1 · Cited by 91 · see citing works
Self-citation
Chemical Evidence for Production of Hydroxyl Radicals During Microsomal Electron Transfer
Cohen, G., & Cederbaum, A. I. (1979) · Science · doi:10.1126/science.432627 · Cited by 90 · see citing works
RADIATION PROTECTION BY SUPEROXIDE DISMUTASE
Petkau, A. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07015.x · Cited by 90 · see citing works
Superoxide dismutase in anaerobes: survey
Gregory, E. M., Moore, W. E., & Holdeman, L. V. (1978) · Applied and Environmental Microbiology · doi:10.1128/aem.35.5.988-991.1978 · Cited by 89 · see citing works
Isolation and characterization of a manganese-containing superoxide dismutase from rat liver
Salin, M. L., Day, E. D., & Crapo, J. D. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90027-9 · Cited by 89 · see citing works
Metal sites of copper-zinc superoxide dismutase
Beem, K. M., Richardson, D. C., & Rajagopalan, K. V. (1977) · Biochemistry · doi:10.1021/bi00628a027 · Cited by 89 · see citing works
Superoxide lon as the cause of the oxygen effect.
Oberley, L. W., Lindgren, L. A., Baker, S. A., & Stevens, R. H. (1976) · PubMed · Cited by 89 · see citing works
Superoxide anion involvement in NBT reduction catalyzed by nadph‐cytochrome P‐450 reductase: A pitfall
Auclair, C., Torrès, M., & Hakim, J. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80514-6 · Cited by 87 · see citing works
The protective action of superoxide dismutase on metal-ion catalysed peroxidation of phospholipids
Gutteridge, J. M. C. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(77)80208-8 · Cited by 86 · see citing works
Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents
Malinowski, D. P., & Fridovich, I. (1979) · Biochemistry · doi:10.1021/bi00590a005 · Cited by 85 · see citing works
Self-citation
Catalytic Mechanism of Cytochrome Oxidase
Antonini, E., Brunori, M., Greenwood, C., et al. (1970) · Nature · doi:10.1038/228936a0 · Cited by 84 · see citing works
Inactivation of Escherichia coli by superoxide radicals and their dismutation products
HEMMEN, J. J. V., & Meuling, W. J. A. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90556-2 · Cited by 84 · see citing works
Superoxide anion as a mediator of drug-induced oxidative hemolysis.
Goldberg, B. D., & Stern, A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81885-7 · Cited by 83 · see citing works
A pulse-radiolysis study of the manganese-containing superoxide dismutase from Bacillus stearothermophilus
McAdam, M. E., Levelle, F., Fox, R. A., & Fielden, E. M. (1977) · Biochemical Journal · doi:10.1042/bj1650081 · Cited by 83 · see citing works
Ferric and manganic superoxide dismutases in Euglena gracilis
Kanematsu, S., & Asada, K. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90380-1 · Cited by 81 · see citing works
Studies related to antitumor antibiotics. Part VII. Synthesis of streptonigrin analogues and their single strand scission of DNA
Lown, J. W., & Sim, S.-K. (1976) · Canadian Journal of Chemistry · doi:10.1139/v76-363 · Cited by 81 · see citing works
The role of superoxide radical in a nonenzymatic hydroxylation
Goscin, S. A., & Fridovich, I. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90398-0 · Cited by 81 · see citing works
Self-citation
Tetrahydropterin Oxidation without Hydroxylation Catalyzed by Rat Liver Phenylalanine Hydroxylase
Fisher, D. B., & Kaufman, S. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43772-1 · Cited by 79 · see citing works
Buffer dependence of carbonic anhydrase catalyzed oxygen-18 exchange at equilibrium
Silverman, D. N., & Tu, C. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00841a045 · Cited by 79 · see citing works
Protection of Post-irradiated Mice by Superoxide Dismutase
Petkau, A., Chelack, W. S., & Pleskach, S. D. (1976) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553007614550341 · Cited by 78 · see citing works
Superoxide Dismutase from Thermus aquaticus
Sato, S., & Harris, J. I. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11328.x · Cited by 77 · see citing works
Hydroxyl radical production in a purified NADPH-cytochrome c (P-450) reductase system
Lai, C.-S., Grover, T. A., & Piette, L. H. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90042-0 · Cited by 76 · see citing works
Effects of the generation of superoxide anion on permeability of liposomes
Goldstein, I. M., & Weissmann, G. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(77)91515-7 · Cited by 76 · see citing works
Reactive forms of oxygen and chemiluminescence in phagocytizing rabbit alveolar macrophages
Miles, P. R., Castranova, V., & Lee, P. (1978) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1978.235.3.c103 · Cited by 75 · see citing works
Physiological function of superoxide dismutase in glucose-limited chemostat cultures of Escherichia coli
Hassan, H. M., & Fridovich, I. (1977) · Journal of Bacteriology · doi:10.1128/jb.130.2.805-811.1977 · Cited by 73 · see citing works
Self-citation
A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii. Enzymologic and spectrophotometric properties.
Kido, T., Soda, K., Suzuki, T., et al. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32932-0 · Cited by 70 · see citing works
The Tiron free radical as a sensitive indicator of chloroplastic photoautoxidation
Miller, R. W., & Macdowall, F. D. H. (1975) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(75)90062-6 · Cited by 69 · see citing works
Purification and properties of superoxide dismutase from a red alga, Porphyridium cruentum.
Misra, H. P., & Fridovich, I. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39975-1 · Cited by 69 · see citing works
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Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
The Free Radical Theory of Aging Matures
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Authors: Fridovich, I.
Affiliations: Duke Medical Center (US)
Corresponding author: Fridovich, Irwin
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 1995-06
Volume: 64
Issue: 1
Pages: 97-112
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.bi.64.070195.000525
OpenAlex: W2114443210
Cited by: 3,455
References: 281
Citations by year: 2026: 66 · 2025: 75 · 2024: 79 · 2023: 90 · 2022: 97 · 2021: 108 · 2020: 90 · 2019: 106 · 2018: 115 · 2017: 124 · 2016: 121 · 2015: 139 · 2014: 166 · 2013: 161 · 2012: 157
FWCI: 15.61
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords: superoxide, superoxide dismutase, Cu/Zn superoxide dismutase, Mn superoxide dismutase, [4Fe-4S] cluster, aconitase, hydroxyl radical generation, peroxidase activity, glycosaminoglycans, nitric oxide, Escherichia coli, soft drinks, sodB, auxotrophy, mutagenesis, DNA damage, yeast, Drosophila, lifespan, manganese complexes
MeSH terms: Animals, Carbohydrates, Escherichia coli, Humans, Mutation, Superoxides, Superoxide Dismutase, Hydroxyl Radical, Carbohydrate Metabolism

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Superoxide radical and superoxide dismutases

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