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

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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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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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