Superoxide-Driven Aconitase FE-S Center Cycling
Abstract
O−2 produced by the autoxidation of respiratory chain electron carriers, and other cellular reductants, inactivates bacterial and mammalian iron-sulfur-containing (de)hydratases including the citric acid cycle enzyme aconitase. Release of the solvent-exposed iron atom and oxidation of the [4Fe-4S]2+ cluster accompanies loss of catalytic activity. Rapid reactivation is achieved by iron-sulfur cluster reduction and Fe2+ insertion. Inactivation-reactivation is a dynamic and cyclical process which modulates aconitase and (de)hydratase activities in Escherichia coli and mammalian cells. The balance of inactive and active aconitase provides a sensitive measure of the changes in steady-statO−2 levels occuring in living cells and mitochondria under stress conditions. Aconitases are also inactivated by other oxidants including O2, H2O2, NO., and ONOO− which are associated with inflammation, hyperoxia and other pathophysiological conditions. Loss of aconitase activity during oxidant stress may impair energy production, and the liberation of reactive iron may further enhance oxidative damage. Iron-sulfur center cycling may also serve adaptive functions by modulating gene expression or by signaling metabolic quiescence.
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Mitochondrial reactive oxygen species may be generated at other sites such as α-ketoglutarate dehydrogenase and iron-sulfur centers in aconitase.
“Mitochondrial ROS may be generated at other sites as well, such as α-ketoglutarate dehydrogenase (6) and the iron–sulfur centers in the aconitase protein, where conversion of superoxide to the hydroxyl radical results in inactivation of the enzyme (110, 319).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [110]
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- Authors
- Gardner, P. R.
- Affiliations
- Cincinnati Children's Hospital Medical Center (US)
- Corresponding author
- Gardner, Paul R.
- ORCID
- Gardner, Paul R.
- Venue
- Bioscience Reports
- Publisher
- Portland Press Ltd.
- Published
- 1997-02-01
- Volume
- 17
- Issue
- 1
- Pages
- 33-42
- ISSN
- 0144-8463 (ISSN-L)
- 1573-4935
- OpenAlex
- W73773881
- Cited by
- 190
- References
- 53
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 6 · 2023: 5 · 2022: 4 · 2021: 5 · 2020: 8 · 2019: 3 · 2018: 7 · 2017: 8 · 2016: 7 · 2015: 6 · 2014: 8 · 2013: 8 · 2012: 9
- FWCI
- 8.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Bioscience Reports (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- American Lung Association
- National Institutes of Health
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- aconitase, iron-sulfur clusters, [4Fe-4S] cluster, superoxide, autoxidation, enzyme inactivation, reactivation, oxidative stress, reactive oxygen species, mitochondrial iron metabolism, Escherichia coli, metabolic quiescence, oxidative damage
- MeSH terms
- Aconitate Hydratase, Animals, Humans, Iron-Sulfur Proteins, Superoxides
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