ReviewMolecular aspects of medicine2022
The peroxidatic activities of Myoglobin and Hemoglobin, their pathological consequences and possible medical interventions.
Review in Molecular aspects of medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 46 citations in OpenAlex.
- Systemic Degree of Perturbation of Plasma Markers Reveals Cumulative Biological Stress Across the Competitive Season in Professional Soccer Players.Sports medicine (Auckland, N.Z.) · 2026Article
- Sunlight-Induced Lipid Oxidation and Degradation of Edible Oil Mediated by Hemoglobin: Implications for Food System Sustainability.Food science & nutrition · 2026Article
- Spectroscopic evaluation of the interaction of myoglobin with biomedically relevant compounds.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Oxidative Characteristics of Turkey Hemoglobin A Containing Covalently Bound Epigallocatechin Gallate.Journal of agricultural and food chemistry · 2026Article
- Therapeutic Potential of Cytoglobin and Neuroglobin in Oxidative Stress-Driven Liver Diseases.Antioxidants (Basel, Switzerland) · 2026Review
- Red Blood Cells in Normal and Pathological States: Redox Reactions of Hemoglobin.Molecules (Basel, Switzerland) · 2026Review
- Serum Myoglobin After Cardiac Surgery Predicts Postoperative Cardiogenic Shock Requiring Mechanical Circulatory Support Within 14 Days.Shock (Augusta, Ga.) · 2026Article
- Development and validation of a prediction model for in-hospital mortality in older adults with acute poisoning.The Journal of international medical research · 2025Article
- Monitoring Inhibition of Hemoglobin Peroxidase Activity After Exposure to Cigarette Smoke Using an Electrochemical Biosensor.Biosensors · 2025Article
- New Approaches and Strategies for the Repurposing of Iron Chelating/Antioxidant Drugs for Diseases of Free Radical Pathology in Medicine.Antioxidants (Basel, Switzerland) · 2025Review
- Impact of Rhabdomyolysis on Clinical Outcomes in Patients With Acute Myocardial Infarction.Cureus · 2025Article
- Boosting nutritional value: the role of iron fortification in meat and meat products.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Review
- Major heme proteins hemoglobin and myoglobin with respect to their roles in oxidative stress - a brief review.Frontiers in chemistry · 2025Review
- The Roles of Oxidative Stress and Red Blood Cells in the Pathology of the Varicose Vein.International journal of molecular sciences · 2024Review
- Reasons why life on Earth rarely makes fluorine-containing compounds and their implications for the search for life beyond Earth.Scientific reports · 2024Article
- Modulation of the Human Erythrocyte Antioxidant System by the 5- and 6-Membered Heterocycle-Based Nitroxides.Molecules (Basel, Switzerland) · 2024Article
- Ferroptosis as an emerging target in sickle cell disease.Current research in toxicology · 2024Article
- Histidine-Bound Dinitrosyl Iron Complexes: Antioxidant and Antiradical Properties.International journal of molecular sciences · 2023Article
- Insights into the function of cytoglobin.Biochemical Society transactions · 2023Review
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Under those pathological conditions in which Myoglobin and Hemoglobin escape their cellular environments and are thus separated from cellular reductive/protective systems, the inherent peroxidase activities of these proteins can be expressed. This activity leads to the formation of the highly oxidizing oxo-ferryl species. Evidence that this happens in vivo is provided by the formation of a covalent bond between the heme group and the protein and this acts as an unambiguous biomarker for the presence of the oxo ferryl form. The peroxidatic activity also leads to the oxidation of lipids, the products of which can be powerful vasoconstrictive agents (e.g. isoprostanes, neuroprostanes). Here we review the evidence that lipid oxidation occurs following rhabdomyolysis and sub-arachnoid hemorrhage and that the products formed from arachidonic acid chains of phospholipids lead, through vasoconstriction, to kidney failure and brain vasospasm. Intervention in these pathological conditions through administration of reducing agents to remove ferryl heme is discussed. Through-protein electron transfer pathways that facilitate ferryl reduction at low reductant concentration have been identified. We conclude with consideration of the therapeutic use of Hemoglobin Based Oxygen carriers and how the toxicity of these may be reduced by engineering such electron transfer pathways into hemoglobin.
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