The DOI matches its Crossref record; 281 of the 281 references it cites were found in a registry or an index.
SUPEROXIDE RADICAL AND SUPEROXIDE DISMUTASES
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 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]
In the citing paper
“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 the citing paper
“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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The sites of superoxide anion generation in higher plant mitochondria
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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
Mechanisms of Oxidation with Oxygen
Taube, H. (1965) · The Journal of General Physiology · doi:10.1085/jgp.49.1.29 · Cited by 145
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
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
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
Self-citationA 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
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
Epel, B. L., & Neumann, J. (1973) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(73)90211-9 · Cited by 133
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
Self-citationIron containing superoxide dismutases from luminous bacteria
Puget, K., & Michelson, A. M. (1974) · Biochimie · doi:10.1016/s0300-9084(74)80019-2 · Cited by 131
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
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
Superoxide dismutase in some obligately anaerobic bacteria
Hewitt, J. A. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80518-7 · Cited by 127
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
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
Saprin, A. N., & Piette, L. H. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90063-7 · Cited by 125
Pick, M. R., Rabani, J., Yost, F., & Fridovich, I. (1974) · Journal of the American Chemical Society · doi:10.1021/ja00830a026 · Cited by 124
Self-citationMcAdam, M. E., Fox, R. A., Lavelle, F., & Fielden, E. M. (1977) · Biochemical Journal · doi:10.1042/bj1650071 · Cited by 123
Halliwell, B. B. (1977) · Biochemical Journal · doi:10.1042/bj1630441 · Cited by 122
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
Self-citationEthylene 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
Morgan, A. R., Cone, R. L., & Terry, M. E. (1976) · Nucleic Acids Research · doi:10.1093/nar/3.5.1139 · Cited by 121
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
Self-citationREACTIONS 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
Czapski, G., & Ilan, Y. A. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb06988.x · Cited by 119
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
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
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
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
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
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
Oxidation-reduction properties of bovine erythrocyte superoxide dismutase
Fee, J. A., & DiCorleto, P. E. (1973) · Biochemistry · doi:10.1021/bi00748a013 · Cited by 111
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
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
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
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
Self-citationGeneration 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
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 106
Self-citationOrme‐Johnson, W. H., & Beinert, H. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90289-7 · Cited by 105
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
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
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
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
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
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
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
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
Rauckman, E. J., Rosen, G. M., & Kitchell, B. B. (1979) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)11537-x · Cited by 95
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
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
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
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
Self-citationFrank, L., Wood, D. L., & Roberts, R. J. (1978) · Biochemical Pharmacology · doi:10.1016/0006-2952(78)90311-8 · Cited by 92
Misra, H. P., & Fridovich, I. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90386-1 · Cited by 91
Self-citationChemical 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
RADIATION PROTECTION BY SUPEROXIDE DISMUTASE
Petkau, A. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07015.x · Cited by 90
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
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
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
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
Auclair, C., Torrès, M., & Hakim, J. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80514-6 · Cited by 87
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
Malinowski, D. P., & Fridovich, I. (1979) · Biochemistry · doi:10.1021/bi00590a005 · Cited by 85
Self-citationCatalytic Mechanism of Cytochrome Oxidase
Antonini, E., Brunori, M., Greenwood, C., et al. (1970) · Nature · doi:10.1038/228936a0 · Cited by 84
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
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
McAdam, M. E., Levelle, F., Fox, R. A., & Fielden, E. M. (1977) · Biochemical Journal · doi:10.1042/bj1650081 · Cited by 83
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
Lown, J. W., & Sim, S.-K. (1976) · Canadian Journal of Chemistry · doi:10.1139/v76-363 · Cited by 81
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
Self-citationTetrahydropterin 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
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
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
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
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
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
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
Hassan, H. M., & Fridovich, I. (1977) · Journal of Bacteriology · doi:10.1128/jb.130.2.805-811.1977 · Cited by 73
Self-citationKido, T., Soda, K., Suzuki, T., et al. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32932-0 · Cited by 70
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
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
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Metadata
- 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
- 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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