Superoxide Dismutases: Ancient Enzymes and New Insights

Miller, Anne-Frances

doi:10.1016/j.febslet.2011.10.048

Cited by 557Metal-Catalyzed Oxygenation MechanismsRedox biology and oxidative stressMetalloenzymes and iron-sulfur proteins

Superoxide Dismutases: Ancient Enzymes and New Insights

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Miller, Anne-Frances·2012·FEBS Letters

DOI 10.1016/j.febslet.2011.10.048PMC PMC5443681

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Abstract

Superoxide dismutases (SODs) catalyze the de toxification of superoxide. SODs therefore acquired great importance as O 2 became prevalent following the evolution of oxygenic photosynthesis. Thus the three forms of SOD provide intriguing insights into the evolution of the organisms and organelles that carry them today. Although ancient organisms employed Fe‐dependent SODs, oxidation of the environment made Fe less bio‐available, and more dangerous. Indeed, modern lineages make greater use of homologous Mn‐dependent SODs. Our studies on the Fe‐substituted MnSOD of Escherichia coli, as well as redox tuning in the FeSOD of E. coli shed light on how evolution accommodated differences between Fe and Mn that would affect SOD performance, in SOD proteins whose activity is specific to one or other metal ion.

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SODs represent a wide group of antioxidant enzymes with complex activities.
“The superoxide dismutases (SODs) represent a wide group of antioxidant enzymes with complex activities [31,32].”
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[5]Miller A-F Que L Jr. Tolman W Superoxide Processing. Coordination Chemistry in the Biosphere and Geosphere 2003 479 506 Pergamon Oxford

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Authors: Miller, A.-F.
Affiliations: University of Kentucky (US)
Corresponding author: Miller, Anne-Frances
ORCID: Miller, Anne-Frances
Venue: FEBS Letters
Publisher: Wiley
Published: 2011-11-10
Volume: 586
Issue: 5
Pages: 585-595
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/j.febslet.2011.10.048
PMC: PMC5443681
OpenAlex: W2020887458
Cited by: 557
References: 104
Citations by year: 2026: 19 · 2025: 41 · 2024: 31 · 2023: 43 · 2022: 63 · 2021: 56 · 2020: 48 · 2019: 54 · 2018: 33 · 2017: 47 · 2016: 35 · 2015: 35 · 2014: 26 · 2013: 18 · 2012: 8
FWCI: 0.39
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (1R01GM085302-01A, R01GM085302)
Topics: Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords: superoxide dismutase, superoxide detoxification, iron superoxide dismutase, Escherichia coli, iron bioavailability, redox tuning, metal ion specificity
MeSH terms: Animals, Eukaryotic Cells, Biological Evolution, Humans, Models, Chemical, Molecular Conformation, Oxidation-Reduction, Prokaryotic Cells, Superoxides, Superoxide Dismutase

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Superoxide Dismutases: Ancient Enzymes and New Insights

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