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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In the citing paper
“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]
Citations
Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citationSuperoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Self-citationMarklund, S. L., & MARKLUND, G. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03714.x · Cited by 10,382
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45228-9 · Cited by 9,097
Self-citationNishikimi, M., Rao, N. A., & Yagi, K. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(72)80218-3 · Cited by 4,091
LXXIII.—Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179
Walling, C. T. (1975) · Accounts of Chemical Research · doi:10.1021/ar50088a003 · Cited by 2,853
Elstner, E. F., & Heupel, A. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90488-7 · Cited by 1,886
Kono, Y. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90479-4 · Cited by 1,787
Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · Journal of the Chemical Society (Resumed) · Cited by 1,498
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The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614
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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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