Superoxide and iron: Partners in crime
Abstract
Superoxide (O2-) poses multiple threats, which are diminished by a family of metalloenzymes, the superoxide dismutases. Among the damaging effects of O2- are direct oxidation of low-molecular-weight reductants; inactivation of a select group of enzymes; and reaction with NO to yield the strong oxidant, peroxynitrite. Of even greater import is the ability of O2- to univalently oxidize the [4 Fe-4 S] clusters of dehydratases, which causes release of iron. The "free" iron, which is kept reduced by cellular reductants, then reduces hydroperoxides to hydroxyl or alkoxyl radicals. Because the "free" iron will preferentially bind to anionic polymers, such as nucleic acids, or to anionic surfaces, such as cell membranes, these radicals will be generated adjacent to these vital targets and will preferentially attack them. O2- and iron can thus be viewed as partners in crime, and reciprocal regulatory effects between iron and O2- may be anticipated. These are discussed.
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O2•− reacts slowly with most molecular targets, although it has been shown to disrupt iron and sulphur group enzymes.
“O2•− reacts slowly with most molecular targets, although it has been shown to disrupt iron and sulphur group enzymes [21].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [21]
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Cited by 219
- Authors
- Liochev, S. I., & Fridovich, I.
- Affiliations
- Duke Medical Center (US)
- Venue
- International Union of Biochemistry and Molecular Biology: Life
- Publisher
- Wiley
- Published
- 1999-08-01
- Volume
- 48
- Issue
- 2
- Pages
- 157-161
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W1972748438
- Cited by
- 219
- References
- 0
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 6 · 2023: 8 · 2022: 8 · 2021: 15 · 2020: 7 · 2019: 9 · 2018: 17 · 2017: 6 · 2016: 10 · 2015: 9 · 2014: 12 · 2013: 11 · 2012: 10
- FWCI
- 2.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- IUBMB Life (publishedVersion)
- PubMed (publishedVersion)
- Funders
- ALS Association
- North Carolina Biotechnology Center
- National Institutes of Health
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- superoxide, iron, superoxide dismutase, peroxynitrite, [4Fe-4S] cluster, dehydratase, iron release, hydroxyl radicals, alkoxy radicals, hydroperoxide reduction, oxidative damage, iron regulation, redox regulation
- MeSH terms
- Escherichia coli, Homeostasis, Hydrogen Peroxide, Iron, Nitrates, Superoxides, Superoxide Dismutase, Gene Deletion
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