ArticleFrontiers in physiology2015
Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity.
Article in Frontiers in physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 49 citations in OpenAlex.
- Trial
- Mock Samples That Mimic Human Cervicovaginal Samples to Accelerate the Development and Evaluation of Assays for High-Risk HPV for Cervical Cancer Screening.Journal of medical virology · 2026Article
- Changes in Fetal Hemoglobin in Very Preterm Infants Born Small for Gestational Age: A Retrospective Observational Study.Children (Basel, Switzerland) · 2026Article
- Fetal Hemoglobin in Preterm Infants After Resuscitation with Immediate Cord Clamping, Delayed Cord Clamping, or Cord Milking.Children (Basel, Switzerland) · 2025Article
- Development and validation of a multivariate nomogram for predicting retinopathy of prematurity in infants with gestational age ≤34 weeks.Frontiers in pediatrics · 2025Article
- Review
- Preparation and Utilization of a Highly Discriminative Absorbent Imprinted with Fetal Hemoglobin.Polymers · 2024Article
- Banked term umbilical cord blood to meet the packed red blood cell transfusion needs of extremely-low-gestational-age neonates: a feasibility analysis.Journal of perinatology : official journal of the California Perinatal Association · 2024Article
- Effect of autologous umbilical cord blood transfusion in the development of retinopathy of prematurity: randomized clinical trial - study protocol.Frontiers in pediatrics · 2023Article
- The Regulated Cell Death and Potential Interventions in Preterm Infants after Intracerebral Hemorrhage.Current neuropharmacology · 2023Review
- Structural and oxidative investigation of a recombinant high-yielding fetal hemoglobin mutant.Frontiers in molecular biosciences · 2023Article
- Low fraction of fetal haemoglobin is associated with retinopathy of prematurity in the very preterm infant.The British journal of ophthalmology · 2022Observational
- Transfusion-Free Survival Predicts Severe Retinopathy in Preterm Neonates.Frontiers in pediatrics · 2022Article
- Stability of Maleimide-PEG and Mono-Sulfone-PEG Conjugation to a Novel Engineered Cysteine in the Human Hemoglobin Alpha Subunit.Frontiers in chemistry · 2021Article
- Rapid Separation of Human Hemoglobin on a Large Scale From Non-clarified Bacterial Cell Homogenates Using Molecularly Imprinted Composite Cryogels.Frontiers in bioengineering and biotechnology · 2021Article
- Interplay Between Plasma Membrane Lipid Alteration, Oxidative Stress and Calcium-Based Mechanism for Extracellular Vesicle Biogenesis From Erythrocytes During Blood Storage.Frontiers in physiology · 2020Article
- Site-directed mutagenesis of cysteine residues alters oxidative stability of fetal hemoglobin.Redox biology · 2018Article
- Comparison of the oxidative reactivity of recombinant fetal and adult human hemoglobin: implications for the design of hemoglobin-based oxygen carriers.Bioscience reports · 2018Article
- The Reaction of Oxy Hemoglobin with Nitrite: Mechanism, Antioxidant-Modulated Effect, and Implications for Blood Substitute Evaluation.Molecules (Basel, Switzerland) · 2018Article
- Effective intermediate-spin iron in OProceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In the presence of excess hydrogen peroxide (H2O2), ferrous (Fe(+2)) human hemoglobin (Hb) (α2β2) undergoes a rapid conversion to a higher oxidation ferryl state (Fe(+4)) which rapidly autoreduces back to the ferric form (Fe(+3)) as H2O2 is consumed in the reaction. In the presence of additional H2O2 the ferric state can form both ferryl Hb and an associated protein radical in a pseudoperoxidative cycle that results in the loss of radicals and heme degradation. We examined whether adult HbA (β2α2) exhibits a different pseudoenzymatic activity than fetal Hb (γ2α2) due to the switch of γ to β subunits. Rapid mixing of the ferric forms of both proteins with excess H2O2 resulted in biphasic kinetic time courses that can be assigned to γ/β and α, respectively. Although there was a 1.5 fold increase in the fast reacting γ /β subunits the slower reacting phases (attributed to α subunits of both proteins) were essentially the same. However, the rate constant for the auto-reduction of ferryl back to ferric for both proteins was found to be 76% higher for HbF than HbA and in the presence of the mild reducing agent, ascorbate there was a 3-fold higher reduction rate in ferryl HbF as opposed to ferryl HbA. Using quantitative mass spectrometry in the presence of H2O2 we found oxidized γ/β Cys93, to be more abundantly present in HbA than HbF, whereas higher levels of nitrated β Tyr35 containing peptides were found in HbA samples treated with nitrite. The extraordinary stability of HbF reported here may explain the evolutionary advantage this protein may confer onto co-inherited hemoglobinopathies and can also be utilized in the engineering of oxidatively stable Hb-based oxygen carriers.
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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.