Autocatalytic radical reactions in physiological prosthetic heme modification
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAutocatalytic Radical Reactions in Physiological Prosthetic Heme ModificationChristophe Colas and Paul R. Ortiz de MontellanoView Author Information Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California 94143-0446 Cite this: Chem. Rev. 2003, 103, 6, 2305–2332Publication Date (Web):April 12, 2003Publication History Received30 September 2002Published online12 April 2003Published inissue 1 June 2003https://pubs.acs.org/doi/10.1021/cr0204303https://doi.org/10.1021/cr0204303research-articleACS PublicationsCopyright © 2003 American Chemical SocietyRequest reuse permissionsArticle Views1036Altmetric-Citations124LEARN 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:Bioinorganic chemistry,Iron,Oxidation,Peptides and proteins,Pyrroles Get e-Alerts
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HO-1 proteolytically degrades haem to yield carbon monoxide, biliverdin, and ferrous iron (Fe2+), which is shuttled to the extracellular fluids by iron exporter ferroportin, present on the cell surfaces of macrophages.
“Haem oxygenase 1 (HO-1) proteolytically degrades haem to yield carbon monoxide, biliverdin, and ferrous iron (Fe2+), which is shuttled to the extracellular fluids by iron exporter ferroportin, present on the cell surfaces of macrophages (Colas and Ortiz De Montellano, 2003; Santos et al., 2003; Pendrak et al., 2004).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Colas and Ortiz De Montellano, 2003
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Diabetes and Kidney Disease: Role of Oxidative Stress
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Iron at the Centre of Candida albicans Interactions
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- Authors
- Colas, C., & Ortiz de Montellano, P. R.
- Affiliations
- University of California, San Francisco (US)
- Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California 94143-0446
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-04-12
- Volume
- 103
- Issue
- 6
- Pages
- 2305-2332
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2072724034
- Cited by
- 139
- References
- 286
- Citations by year
- 2026: 3 · 2025: 1 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 9 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 6 · 2013: 5 · 2012: 7
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-32488, GM 25515, R01GM032488)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK30297, R01DK030297)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Materials Science › Materials Chemistry › Porphyrin and Phthalocyanine Chemistry
- Keywords
- heme modification, heme oxidation, iron oxidation, heme proteins
- MeSH terms
- Base Sequence, Binding Sites, Catalysis, Cytochrome P-450 Enzyme System, Free Radicals, Heme, Heme Oxygenase (Decyclizing), Humans, Molecular Sequence Data, Protein Structure, Secondary
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