ArticleFree radical biology & medicine2013
Myeloperoxidase acts as a source of free iron during steady-state catalysis by a feedback inhibitory pathway.
Article in Free radical biology & medicine, 2013. 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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Who cites it
26 citing papers in PubMed, 62 citations in OpenAlex.
- Salidroside in heavy metal toxicity: a mechanistic review of antioxidant, anti-inflammatory, and anti-apoptotic pathways.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- Electrolyzed Water as a Biocide in Premise Water Networks: A Narrative Review and a Conceptual Framework.Pathogens (Basel, Switzerland) · 2026Review
- Article
- Nutritional deficiencies that may predispose to long COVID.Inflammopharmacology · 2023Review
- Non-Canonical Functions of Myeloperoxidase in Immune Regulation, Tissue Inflammation and Cancer.International journal of molecular sciences · 2022Review
- The relationship between peripheral immune response and disease severity in SARS-CoV-2-infected subjects: A cross-sectional study.Immunology · 2022Article
- Essential Protective Role of Catalytically Active Antibodies (Abzymes) with Redox Antioxidant Functions in Animals and Humans.International journal of molecular sciences · 2022Review
- Hypochlorous Acid: From Innate Immune Factor and Environmental Toxicant to Chemopreventive Agent Targeting Solar UV-Induced Skin Cancer.Frontiers in oncology · 2022Review
- Quantitative proteomics by iTRAQ-PRM based reveals the new characterization for gout.Proteome science · 2021Article
- Melatonin interferes with COVID-19 at several distinct ROS-related steps.Journal of inorganic biochemistry · 2021Review
- A Multiple-Hit Hypothesis Involving Reactive Oxygen Species and Myeloperoxidase Explains Clinical Deterioration and Fatality in COVID-19.International journal of biological sciences · 2021Review
- Inhibition of complement activation, myeloperoxidase, NET formation and oxidant activity by PIC1 peptide variants.PloS one · 2019Article
- Myeloperoxidase deficiency attenuates systemic and dietary iron-induced adverse effects.The Journal of nutritional biochemistry · 2018Article
- Melatonin prevents hypochlorous acid-mediated cyanocobalamin destruction and cyanogen chloride generation.Journal of pineal research · 2018Article
- Mesna (2-mercaptoethane sodium sulfonate) functions as a regulator of myeloperoxidase.Free radical biology & medicine · 2017Article
- Peptide Inhibitor of Complement C1 Inhibits the Peroxidase Activity of Hemoglobin and Myoglobin.International journal of peptides · 2017Article
- Inhibition of Myeloperoxidase Activity in Cystic Fibrosis Sputum by Peptide Inhibitor of Complement C1 (PIC1).PloS one · 2017Article
- Lipocalin 2 alleviates iron toxicity by facilitating hypoferremia of inflammation and limiting catalytic iron generation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2016Article
- Epigallocatechin-3-Gallate Inhibition of Myeloperoxidase and Its Counter-Regulation by Dietary Iron and Lipocalin 2 in Murine Model of Gut Inflammation.The American journal of pathology · 2016Article
- The Defensive Role of Cumulus Cells Against Reactive Oxygen Species Insult in Metaphase II Mouse Oocytes.Reproductive sciences (Thousand Oaks, Calif.) · 2016Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Myeloperoxidase (MPO) is a heme-containing enzyme that generates hypochlorous acid (HOCl) from chloride (Cl(-)) and hydrogen peroxide (H₂O₂). It is implicated in the pathology of several chronic inflammatory conditions such as cardiovascular and pulmonary diseases and cancer. Recently we have shown that HOCl can destroy the heme prosthetic group of hemoproteins. Here, we investigated whether the HOCl formed during steady-state catalysis is able to destroy the MPO heme moiety and thereby function as a major source of free iron. UV-visible spectra and H₂O₂-specific electrode measurements recorded during steady-state HOCl synthesis by MPO showed that the degree of MPO heme destruction increased after multiple additions of H₂O₂ (10 µM), precluding the enzyme from functioning at maximum activity (80-90% inhibition). MPO heme destruction occurred only in the presence of Cl(-). Stopped-flow measurements revealed that the HOCl-mediated MPO heme destruction was complex and occurred through transient ferric species whose formation and decay kinetics indicated it participates in heme destruction along with subsequent free iron release. MPO heme depletion was confirmed by the buildup of free iron utilizing the ferrozine assay. Hypochlorous acid, once generated, first equilibrates in the solution as a whole before binding to the heme iron and initiating heme destruction. Eliminating HOCl from the MPO milieu by scavenging HOCl, destabilizing the MPO-Compound I-Cl complex that could be formed during catalysis, and/or inhibiting MPO catalytic activity partially or completely protects MPO from HOCl insults. Collectively, this study elucidates the bidirectional relationship between MPO and HOCl, which highlights the potential role of MPO as a source of free iron.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.