Cited by 823Metal-Catalyzed Oxygenation MechanismsChemical Reaction MechanismsMetalloenzymes and iron-sulfur proteins

Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?

Stubbe, JoAnne, Nocera, Daniel G., Yee, Cyril S., Chang, Michelle C. Y.·2003·Chemical Reviews

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRadical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?JoAnne Stubbe, Daniel G. Nocera, Cyril S. Yee, and Michelle C. Y. ChangView Author Information Department of Chemistry, 77 Massachusetts Avenue, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307 Cite this: Chem. Rev. 2003, 103, 6, 2167–2202Publication Date (Web):May 24, 2003Publication History Received16 January 2003Published online24 May 2003Published inissue 1 June 2003https://pubs.acs.org/doi/10.1021/cr020421uhttps://doi.org/10.1021/cr020421uresearch-articleACS PublicationsCopyright © 2003 American Chemical SocietyRequest reuse permissionsArticle Views7657Altmetric-Citations730LEARN 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:Charge transfer,Genetics,Monomers,Peptides and proteins,Redox reactions Get e-Alerts

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  • Proton-coupled electron transfer mechanisms have been shown to underlie amino acid radical generation and transport.

    “In biological energy storage, the importance of proton translocation driven by electron transfer was first noted in 1961 [89], and since then, proton-coupled electron transfer mechanisms [90] have been shown to underlie amino acid radical generation and transport [91] along with the activation of most substrate bonds at enzyme-active sites [92].”

    From The future of quantum biology (2018) · cites this paper as [91]

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Authors
Stubbe, J., Nocera, D. G., Yee, C. S., & Chang, M. C. Y.
Affiliations
Massachusetts Institute of Technology (US)
Corresponding author
Nocera, Daniel G.
Venue
Chemical Reviews
Published
2003-05-24
Volume
103
Issue
6
Pages
2167-2202
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2002551641
Cited by
823
References
328
Citations by year
2026: 12 · 2025: 24 · 2024: 24 · 2023: 21 · 2022: 24 · 2021: 24 · 2020: 21 · 2019: 22 · 2018: 32 · 2017: 30 · 2016: 28 · 2015: 46 · 2014: 41 · 2013: 53 · 2012: 71
FWCI
2.65
Type
journal article
Language
en
Open access
closed
Locations
  • Chemical Reviews (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (GM29595, GM47274, R01GM047274)
Topics
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
class I ribonucleotide reductase, radical initiation, charge transfer, redox reactions, enzyme mechanism, thymidine biosynthesis
MeSH terms
DNA, DNA Repair, DNA Replication, Electron Transport, Escherichia coli, Free Radicals, Models, Molecular, Ribonucleotide Reductases, Mutagenesis, Site-Directed

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