Iron–sulfur proteins with nonredox functions

Flint, Dennis H.; Allen, Ronda M.

doi:10.1021/cr950041r

Cited by 280Metalloenzymes and iron-sulfur proteinsEnzyme Structure and FunctionMetal-Catalyzed Oxygenation Mechanisms

Iron–sulfur proteins with nonredox functions

Flint, Dennis H., Allen, Ronda M.·1996·Chemical Reviews

DOI 10.1021/cr950041r

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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIron−Sulfur Proteins with Nonredox FunctionsDennis H. Flint and Ronda M. AllenView Author Information E. I. du Pont de Nemours and Co., Central Research and Development, Experimental Station, P.O. Box 80328, Wilmington, Delaware 19880-0328 Cite this: Chem. Rev. 1996, 96, 7, 2315–2334Publication Date (Web):November 7, 1996Publication History Received14 February 1996Revised28 May 1996Published online7 November 1996Published inissue 1 January 1996https://pubs.acs.org/doi/10.1021/cr950041rhttps://doi.org/10.1021/cr950041rresearch-articleACS PublicationsCopyright © 1996 American Chemical SocietyRequest reuse permissionsArticle Views2297Altmetric-Citations237LEARN 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 InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Cluster chemistry,Iron,Iron-sulfur clusters,Monomers,Peptides and proteins Get e-Alerts

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The high reactivity of aconitase with superoxide ion is due to the presence of the [4Fe-4S] centre with labile Fe in its active site.
“The high reactivity of aconitase with superoxide ion is due to the presence of the [4Fe-4S] centre with labile Fe in its active site [113].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [113]
The mechanism of aconitase reaction with superoxide involves electrostatic attraction, protonation to a strong univalent oxidant, and single electron abstraction.
“The mechanism involves (i) electrostatic attraction of the superoxide to the solvent-exposed group, (ii) protonation to become a strong univalent oxidant, and (iii) single electron abstraction.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [113]
The reactivity of aconitase with superoxide is attributed to electrophilic Fe, large nucleophilicity of O2•−, increased oxidative potential of iron-bound O2•−, and sensitivity of Fe-S bonds to oxidation.
“The reactivity is attributed to the electrophilic character of Fe, the large nucleophilicity of O2•−, the increased oxidative potential of O2•− in its iron-bound state and the sensitivity of Fe-S bonds to oxidation [113].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [113]

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Authors: Flint, D. H., & Allen, R. M.
Affiliations: DuPont (United States) (US)
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 1996-01-01
Volume: 96
Issue: 7
Pages: 2315-2334
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/cr950041r
OpenAlex: W2952306726
Cited by: 280
References: 157
Citations by year: 2026: 3 · 2025: 8 · 2024: 10 · 2023: 9 · 2022: 11 · 2021: 8 · 2020: 12 · 2019: 11 · 2018: 8 · 2017: 7 · 2016: 8 · 2015: 8 · 2014: 16 · 2013: 8 · 2012: 6
FWCI: 0.93
Type: journal article
Language: en
Open access: closed
Locations: Chemical Reviews (publishedVersion)
PubMed (publishedVersion)
Topics: Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords: iron-sulfur proteins, iron-sulfur clusters, cluster chemistry

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Iron–sulfur proteins with nonredox functions

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