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Cited by 1,081Metal-Catalyzed Oxygenation MechanismsRedox biology and oxidative stressMetalloenzymes and iron-sulfur proteins

Superoxide dismutases and superoxide reductases

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Sheng, Yuewei, Abreu, Isabel A., Cabelli, Diane E., Maroney, Michael J., Miller, Anne-Frances, Teixeira, Miguel, Valentine, Joan Selverstone·2014·Chemical Reviews
DOI 10.1021/cr4005296PMC PMC4317059
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTSuperoxide Dismutases and Superoxide ReductasesYuewei Sheng†, Isabel A. Abreu*‡§, Diane E. Cabelli*∥, Michael J. Maroney*⊥, Anne-Frances Miller*#, Miguel Teixeira*‡, and Joan Selverstone Valentine*†∇View Author Information† Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, California 90095, United States‡ Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal§ Instituto de Biologia Experimental e Tecnológica, Av. da República, Qta. do Marquês, Estação Agronómica Nacional, Edificio IBET/ITQB, 2780-157, Oeiras, Portugal∥ Chemistry Department, Brookhaven National Laboratory, Upton, New York 11973, United States⊥ Department of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States# Department of Chemistry, University of Kentucky, Lexington, Kentucky 40506-0055, United States∇ Department of Bioinspired Sciences, Ewha Womans University, Seoul 120-750, Republic of Korea*E-mail: [email protected]*E-mail: [email protected]*E-mail: [email protected]*E-mail: [email protected]*E-mail: [email protected]*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 7, 3854–3918Publication Date (Web):April 1, 2014Publication History Received24 September 2013Published online1 April 2014Published inissue 9 April 2014https://doi.org/10.1021/cr4005296Copyright © 2014 American Chemical SocietyRIGHTS & PERMISSIONSACS AuthorChoiceArticle Views20491Altmetric-Citations581LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (31 MB) Get e-AlertsSUBJECTS:Ligands,Metals,Monomers,Peptides and proteins,Redox reactions Get e-Alerts

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  • SOR and SOD enzymes have the ability to react selectively with superoxide in both the oxidised and reduced SOD and SOR states.

    “OR and SOD enzymes have the ability to react selectively with superoxide in both the oxidised and reduced SOD and SOR states [69].”

    From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [69]

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Authors
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S.
Affiliations
  • University of California, Los Angeles (US)
  • Instituto de Biologia Experimental e Tecnológica (PT)
  • Brookhaven National Laboratory (US)
  • University of Massachusetts Amherst (US)
  • University of Kentucky (US)
  • Instituto de Tecnologia Química e Biológica António Xavier (PT)
  • Ewha Womans University (KR)
Corresponding author
  • Abreu, Isabel A.
  • Cabelli, Diane E.
  • Maroney, Michael J.
  • Miller, Anne-Frances
  • Teixeira, Miguel
  • Valentine, Joan Selverstone
ORCID
Venue
Chemical Reviews
Publisher
American Chemical Society (ACS)
Published
2014-04-01
Volume
114
Issue
7
Pages
3854-3918
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
DOI
10.1021/cr4005296
PMC
PMC4317059
OpenAlex
W1965970124
Cited by
1,081
References
596
Citations by year
2026: 83 · 2025: 136 · 2024: 147 · 2023: 125 · 2022: 121 · 2021: 87 · 2020: 88 · 2019: 84 · 2018: 64 · 2017: 57 · 2016: 35 · 2015: 37 · 2014: 15 · 2013: 1
FWCI
1.06
Type
journal article
Language
en
Open access
Licence
Locations
  • Chemical Reviews (publishedVersion, other-oa)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institute of General Medical Sciences (GM-28222, R01GM028222, R01GM069696, R01GM085302)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK46826)
  • National Institute of Neurological Disorders and Stroke (P01NS049134)
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 reductase, superoxide, reactive oxygen species, metalloenzymes, manganese, iron, enzyme mechanism, redox chemistry, metallochelates, metalloproteins
MeSH terms
Hydrogen-Ion Concentration, Kinetics, Oxidoreductases, Superoxides, Superoxide Dismutase, Catalytic Domain, Biocatalysis

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