Cited by 189Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsHeme Oxygenase-1 and Carbon Monoxide

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The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Reeder, Brandon J.·2010·Antioxidants & Redox Signaling

DOI 10.1089/ars.2009.2974

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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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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
DOI: 10.1089/ars.2009.2974
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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The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

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