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

Reeder, Brandon J.

doi:10.1089/ars.2009.2974

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

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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The reaction between H2O2 and both ferrous and ferric hemoglobin results in heme degradation and release of free iron.
“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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Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
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Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
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Protective Role for Antioxidants in Acute Kidney Disease
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Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries
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Haptoglobin
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Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control
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Heme as a Target for Therapeutic Interventions
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Development of Recombinant Hemoglobin-Based Oxygen Carriers
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Post-infarct cardiac rupture: Recent insights on pathogenesis and therapeutic interventions
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Nitrite Reduction and Cardiovascular Protection
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Protective Role of Nrf2 in Renal Disease
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Determination of extinction coefficients of human hemoglobin in various redox states
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Hemoglobin and Red Blood Cells Catalyze Atom Transfer Radical Polymerization
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Role of Heme Oxygenase as a Modulator of Heme-Mediated Pathways
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Redox Reactions of Myoglobin
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Haptoglobin: Old protein with new functions
Alayash, A. I. (2010) · Clinica Chimica Acta · doi:10.1016/j.cca.2010.12.011 · Cited by 99 · see citing works
Mechanisms of Toxicity and Modulation of Hemoglobin-based Oxygen Carriers
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Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for α 1 -Microglobulin
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Cell-free hemoglobin: a novel mediator of acute lung injury
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Hemolysis Derived Products Toxicity and Endothelium: Model of the Second Hit
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The effect of dietary nitrate supplementation on the oxygen cost of cycling, walking performance and resting blood pressure in individuals with chronic obstructive pulmonary disease: A double blind placebo controlled, randomised control trial
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The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane
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Heme Catabolic Pathway in Inflammation and Immune Disorders
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Dgat1 and Dgat2 regulate enterocyte triacylglycerol distribution and alter proteins associated with cytoplasmic lipid droplets in response to dietary fat
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Cytoglobin: biochemical, functional and clinical perspective of the newest member of the globin family
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Erythrocyte metabolism
Chatzinikolaou, P. N., Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Vrabas, I. S., Kyparos, A., D’Alessandro, A., & Nikolaidis, M. G. (2024) · Acta Physiologica · doi:10.1111/apha.14081 · Cited by 74 · see citing works
Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase‐1
Kassa, T., Jana, S., Meng, F., & Alayash, A. I. (2016) · FEBS Open Bio · doi:10.1002/2211-5463.12103 · Cited by 71 · see citing works
Molecular Controls of the Oxygenation and Redox Reactions of Hemoglobin
Bonaventura, C., Henkens, R. W., Alayash, A. I., Banerjee, S., & Crumbliss, A. L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4947 · Cited by 70 · see citing works
Hemoglobin-Based Blood Substitutes and the Treatment of Sickle Cell Disease: More Harm than Help?
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Repurposing Biocatalysts to Control Radical Polymerizations
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Treating itch in psoriasis.
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Hypoxic survival requires a 2-on-2 hemoglobin in a process involving nitric oxide
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Redox phospholipidomics of enzymatically generated oxygenated phospholipids as specific signals of programmed cell death
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Neuronal Hemoglobin Expression and Its Relevance to Multiple Sclerosis Neuropathology
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Oxidative pathways in the sickle cell and beyond
Alayash, A. I. (2017) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2017.05.009 · Cited by 63 · see citing works
Redox properties of human hemoglobin in complex with fractionated dimeric and polymeric human haptoglobin
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Cytoglobin modulates myogenic progenitor cell viability and muscle regeneration
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Myoglobin and Polydopamine‐Engineered Raman Nanoprobes for Detecting, Imaging, and Monitoring Reactive Oxygen Species in Biological Samples and Living Cells
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Functional differentiation of myoglobin isoforms in hypoxia-tolerant carp indicates tissue-specific protective roles
Helbo, S., Dewilde, S., Williams, D. R., Berghmans, H., Berenbrink, M., Cossins, A. R., & Fago, A. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00501.2011 · Cited by 57 · see citing works
Sickle Cell Hemoglobin in the Ferryl State Promotes βCys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10)
Kassa, T., Jana, S., Strader, M. B., Meng, F., Jia, Y., Wilson, M. T., & Alayash, A. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.651257 · Cited by 57 · see citing works
The peroxidatic activities of Myoglobin and Hemoglobin, their pathological consequences and possible medical interventions
Wilson, M. T., & Reeder, B. J. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101045 · Cited by 56 · see citing works
Self-citation
Oxidative insult can induce malaria-protective trait of sickle and fetal erythrocytes
Cyrklaff, M., Srismith, S., Nyboer, B., Burda, K., Hoffmann, A., Lasitschka, F., Adjalley, S. H., Bisseyé, C., Simporè, J., Mueller, A., et al. (2016) · Nature Communications · doi:10.1038/ncomms13401 · Cited by 56 · see citing works
Haemoglobin causes neuronal damage in vivo which is preventable by haptoglobin
Garland, P., Morton, M. J., Haskins, W., Zolnourian, A. H., Durnford, A. J., Gaastra, B., Toombs, J., Heslegrave, A., More, J. E., Okemefuna, A. I., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcz053 · Cited by 55 · see citing works
Extracellular hemoglobin: the case of a friend turned foe
Quaye, I. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00096 · Cited by 53 · see citing works
Independent association of HbA1c and nonalcoholic fatty liver disease in an elderly Chinese population
Ma, H., Xu, C., Xu, L., Yu, C., Miao, M., & Li, Y. (2013) · BMC Gastroenterology · doi:10.1186/1471-230x-13-3 · Cited by 54 · see citing works
Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes
Xiao, Q., Jiang, X., Moore, K. J., Shao, Y., Pi, H., Dubail, I., Charbit, A., Newton, S. M., & Klebba, P. E. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07667.x · Cited by 51 · see citing works
Hemoglobin S Polymerization and Red Cell Membrane Changes
Kuypers, F. A. (2014) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2013.12.002 · Cited by 51 · see citing works
Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity
Ratanasopa, K., Strader, M. B., Alayash, A. I., & Bülow, L. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00039 · Cited by 50 · see citing works
Allogeneic cord blood transfusions prevent fetal haemoglobin depletion in preterm neonates. Results of the CB‐TrIP study
Teofili, L., Papacci, P., Orlando, N., Bianchi, M., Molisso, A., Purcaro, V., Valentini, C. G., Giannantonio, C., Serrao, F., Chiusolo, P., et al. (2020) · British Journal of Haematology · doi:10.1111/bjh.16851 · Cited by 49 · see citing works
Oxidized Ferric and Ferryl Forms of Hemoglobin Trigger Mitochondrial Dysfunction and Injury in Alveolar Type I Cells
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Structural determinants for the formation of sulfhemeprotein complexes
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Extracellular Hemoglobin: Modulation of Cellular Functions and Pathophysiological Effects
Drvenica, I. T., Stančić, A. Z., Maslovarić, I. S., Trivanović, D. I., & Ilić, V. L. (2022) · Biomolecules · doi:10.3390/biom12111708 · Cited by 46 · see citing works
Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity
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Characterization of THB1, a Chlamydomonas reinhardtii Truncated Hemoglobin: Linkage to Nitrogen Metabolism and Identification of Lysine as the Distal Heme Ligand
Johnson, E. A., Rice, S. L., Preimesberger, M. R., Nye, D. B., Gilevicius, L., Wenke, B. B., Brown, J., Witman, G. B., & Lecomte, J. T. J. (2014) · Biochemistry · doi:10.1021/bi5005206 · Cited by 44 · see citing works
A redox signalling globin is essential for reproduction in Caenorhabditis elegans
Henau, S. D., Tilleman, L., Vangheel, M., Luyckx, E., Trashin, S., Pauwels, M., Germani, F., Vlaeminck, C., Vanfleteren, J. R., Bert, W., et al. (2015) · Nature Communications · doi:10.1038/ncomms9782 · Cited by 44 · see citing works
Antimalarial NADPH-Consuming Redox-Cyclers As Superior Glucose-6-Phosphate Dehydrogenase Deficiency Copycats
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Post-translational modification as a response to cellular stress induced by hemoglobin oxidation in sickle cell disease
Strader, M. B., Jana, S., Meng, F., Heaven, M. R., Shet, A. S., Thein, S. L., & Alayash, A. I. (2020) · Scientific Reports · doi:10.1038/s41598-020-71096-6 · Cited by 40 · see citing works
Skeletal muscle heme oxygenase-1 activity regulates aerobic capacity
de Souza, R. W. A., Gallo, D. J., Lee, G. R., Katsuyama, E., Schaufler, A., Weber, J., Csizmadia, E., Tsokos, G. C., Koch, L. G., Britton, S. L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109018 · Cited by 42 · see citing works
Trapping of Human Hemoglobin by Haptoglobin: Molecular Mechanisms and Clinical Applications
Ratanasopa, K., Chakane, S., Ilyas, M., Nantasenamat, C., & Bülow, L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4878 · Cited by 42 · see citing works
Hydrogen Sulfide Abrogates Hemoglobin‐Lipid Interaction in Atherosclerotic Lesion
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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 › Cell Biology › 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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