The DOI matches its Crossref record; 99 of the 99 references it cites were found in a registry or an index.
Superoxide dismutases—a review of the metal-associated mechanistic variations
Abstract
Superoxide dismutases are enzymes that function to catalytically convert superoxide radical to oxygen and hydrogen peroxide. These enzymes carry out catalysis at near diffusion controlled rate constants via a general mechanism that involves the sequential reduction and oxidation of the metal center, with the concomitant oxidation and reduction of superoxide radicals. That the catalytically active metal can be copper, iron, manganese or, recently, nickel is one of the fascinating features of this class of enzymes. In this review, we describe these enzymes in terms of the details of their catalytic properties, with an emphasis on the mechanistic differences between the enzymes. The focus here will be concentrated mainly on two of these enzymes, copper, zinc superoxide dismutase and manganese superoxide dismutase, and some relatively subtle variations in the mechanisms by which they function.
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“It is a prokaryotic enzyme, discovered in some bacterial cells and in the cytosol of plants [86].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [86]
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Cites
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Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
The Copper Chaperone for Superoxide Dismutase
Culotta, V., Klomp, L. W. J., Strain, J. J., Casareno, R. L. B., Krems, B., & Gitlin, J. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23469 · Cited by 851
COPPER-ZINC SUPEROXIDE DISMUTASE AND AMYOTROPHIC LATERAL SCLEROSIS
Valentine, J. S., Doucette, P. A., & Potter, S. Z. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161647 · Cited by 790
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Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
Wiedau‐Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 720
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Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases
Fukai, T., & Ushio‐Fukai, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3999 · Cited by 2,074
Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130
Superoxide dismutases and superoxide reductases
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081
Self-citation
Metadata
- Authors
- Abreu, I. A., & Cabelli, D. E.
- Affiliations
- Universidade Nova de Lisboa (PT)
- Brookhaven National Laboratory (US)
- Corresponding author
- Cabelli, Diane E.
- ORCID
- Abreu, Isabel A.
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 1804
- Issue
- 2
- Pages
- 263-274
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2028661305
- Cited by
- 563
- References
- 99
- Citations by year
- 2026: 26 · 2025: 44 · 2024: 31 · 2023: 41 · 2022: 47 · 2021: 60 · 2020: 34 · 2019: 38 · 2018: 35 · 2017: 43 · 2016: 43 · 2015: 26 · 2014: 30 · 2013: 19 · 2012: 20
- FWCI
- 0.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fundação para a Ciência e a Tecnologia
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- superoxide dismutase, copper-zinc superoxide dismutase, manganese superoxide dismutase, enzyme mechanism, metalloenzyme catalysis, superoxide, hydrogen peroxide production, copper, iron, manganese, nickel, diffusion-controlled rate constants
- MeSH terms
- Animals, Copper, Humans, Iron, Manganese, Superoxide Dismutase, Zinc, Biocatalysis
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