The DOI matches its Crossref record; 297 of the 297 references it cites were found in a registry or an index.
The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms
Abstract
Pentacoordinate respiratory hemoproteins such as hemoglobin and myoglobin have evolved to supply cells with oxygen. However, these respiratory heme proteins are also known to function as redox enzymes, reacting with compounds such as nitric oxide and peroxides. The recent discoveries of hexacoordinate hemoglobins in vertebrates and nonsymbiotic plants suggest that the redox activity of globins is inherent to the molecule. The uncontrolled formation of radical species resulting from such redox chemistry on respiratory hemoproteins can lead to oxidative damage and cellular toxicity. In this review, we examine the functions of various globins and the mechanisms by which these globins act as redox enzymes under physiologic conditions. Evidence that redox reactions also occur under disease conditions, leading to pathologic complications, also is examined, focusing on recent discoveries showing that the ferryl oxidation state of these hemoproteins is present in these disease states in vivo. In addition, we review the latest advances in the understanding of globin redox mechanisms and how they might affect cellular signaling pathways and how they might be controlled therapeutically or, in the case of hemoglobin-based blood substitutes, through rational design.
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“Another important oxidative pathway is the reaction between H2O2 and both ferrous and ferric Hb, resulting in heme degradation and release of free iron (3), as described in detail in an older comprehensive review by Reeder (150).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [150]
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Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469
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Metadata
- Authors
- Reeder, B. J.
- Affiliations
- University of Essex (GB)
- Corresponding author
- Reeder, Brandon J.
- ORCID
- Reeder, Brandon J.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2010-10
- Volume
- 13
- Issue
- 7
- Pages
- 1087-1123
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2024968752
- Cited by
- 189
- References
- 294
- Citations by year
- 2026: 9 · 2025: 5 · 2024: 7 · 2023: 11 · 2022: 11 · 2021: 11 · 2020: 12 · 2019: 11 · 2018: 7 · 2017: 20 · 2016: 19 · 2015: 15 · 2014: 13 · 2013: 14 · 2012: 13
- FWCI
- 1.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Open Access at Essex (University of Essex) (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Keywords
- hemoglobin, myoglobin, globin, oxidative enzymes, heme proteins, nitric oxide, peroxides, ferryl hemoglobin, oxidative damage, cytotoxicity, signal transduction, hemoglobin-based blood substitutes, plant hemoglobin
- MeSH terms
- Neuroglobin, Cytoglobin, Animals, Blood Substitutes, Globins, Heme, Hemeproteins, Hemoglobins, Humans, Myoglobin, Nerve Tissue Proteins, Nitric Oxide, Oxidation-Reduction, Oxygen, Peroxides, Signal Transduction
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