Cited by 190Metalloenzymes and iron-sulfur proteinsMitochondrial Function and PathologyRedox biology and oxidative stress

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Superoxide-Driven Aconitase FE-S Center Cycling

Gardner, Paul R.·1997·Bioscience Reports

DOI 10.1023/a:1027383100936

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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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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
DOI: 10.1023/a:1027383100936
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: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › 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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