The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
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 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]
Citations
Cites
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor
Gryglewski, R. J., Palmer, R. M. J., & Moncada, S. (1986) · Nature · doi:10.1038/320454a0 · Cited by 2,400
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
Biological effects of the superoxide radical
Fridovich, I. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90526-6 · Cited by 1,420
Regulating the fate of mRNA: the control of cellular iron metabolism
Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210
Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism
Wong, G. H. W., & Goeddel, D. V. (1988) · Science · doi:10.1126/science.3263703 · Cited by 914
Wong, G. H. W., Elwell, J. H., Oberley, L. W., & Goeddel, D. V. (1989) · Cell · doi:10.1016/0092-8674(89)90944-6 · Cited by 802
The inactivation of Fe-S cluster containing hydro-lyases by superoxide
Flint, D. H., Tuminello, J. F., & Emptage, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41538-4 · Cited by 637
Bagg, A., & Neilands, J. B. (1987) · Biochemistry · doi:10.1021/bi00391a039 · Cited by 593
Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.
Castro, L., Rodriguez, M., & Radi, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43894-x · Cited by 589
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Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,651
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Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,681
Guidelines for measuring reactive oxygen species and oxidative damage in cells and in vivo
Murphy, M. P., Bayir, H., Belousov, V., Chang, C. J., Davies, K. J. A., Davies, M. J., Dick, T. P., Finkel, T., Forman, H. J., Janssen-Heininger, Y., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00591-z · Cited by 1,514
Edris, A. E. (2007) · Phytotherapy Research · doi:10.1002/ptr.2072 · Cited by 1,264
Reactive oxygen species and the free radical theory of aging
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Metadata
- 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
- 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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