ArticleThe Journal of biological chemistry2013
α-Hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of α-subunits of human HbA with hydrogen peroxide.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- AAPH-induced oxidative damage reduced anion exchanger 1 (SLC4A1/AE1) activity in human red blood cells: protective effect of an anthocyanin-rich extract.Frontiers in physiology · 2023Article
- Physiology and Proteomic Basis of Lung Adaptation to High-Altitude Hypoxia in Tibetan Sheep.Animals : an open access journal from MDPI · 2022Article
- The role of globins in cardiovascular physiology.Physiological reviews · 2022Review
- Redox-Regulation of α-Globin in Vascular Physiology.Antioxidants (Basel, Switzerland) · 2022Article
- A Long-Term Stable Sensor Based on Fe@PCN-224 for Rapid and Quantitative Detection of HFoods (Basel, Switzerland) · 2021Article
- The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.Biophysical journal · 2020Article
- Alpha-hemoglobin-stabilizing protein (AHSP): a modulatory factor in β-thalassemia.International journal of hematology · 2020Review
- Mechanisms of Toxicity and Modulation of Hemoglobin-based Oxygen Carriers.Shock (Augusta, Ga.) · 2019Review
- Hemoglobin oxidation-dependent reactions promote interactions with band 3 and oxidative changes in sickle cell-derived microparticles.JCI insight · 2018Article
- Endothelial cell α-globin and its molecular chaperone α-hemoglobin-stabilizing protein regulate arteriolar contractility.The Journal of clinical investigation · 2018Article
- Targeting βCys93 in hemoglobin S with an antisickling agent possessing dual allosteric and antioxidant effects.Metallomics : integrated biometal science · 2017Article
- Exploring Oxidative Reactions in Hemoglobin Variants Using Mass Spectrometry: Lessons for Engineering Oxidatively Stable Oxygen Therapeutics.Antioxidants & redox signaling · 2017Review
- Iron accelerates hemoglobin oxidation increasing mortality in vascular diseased guinea pigs following transfusion of stored blood.JCI insight · 2017Article
- Determination of extinction coefficients of human hemoglobin in various redox states.Analytical biochemistry · 2017Article
- Article
- Sickle Cell Hemoglobin in the Ferryl State Promotes βCys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10).The Journal of biological chemistry · 2015Article
- Haptoglobin attenuates hemoglobin-induced heme oxygenase-1 in renal proximal tubule cells and kidneys of a mouse model of sickle cell disease.Blood cells, molecules & diseases · 2015Article
- Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity.Frontiers in physiology · 2015Article
- Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobin.The Journal of biological chemistry · 2014Article
- Redox properties of human hemoglobin in complex with fractionated dimeric and polymeric human haptoglobin.Free radical biology & medicine · 2014Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
α-Hemoglobin stabilizing protein (AHSP) is a molecular chaperone that binds monomeric α-subunits of human hemoglobin A (HbA) and modulates heme iron oxidation and subunit folding states. Although AHSP·αHb complexes autoxidize more rapidly than HbA, the redox mechanisms appear to be similar. Both metHbA and isolated met-β-subunits undergo further oxidation in the presence of hydrogen peroxide (H(2)O(2)) to form ferryl heme species. Surprisingly, much lower levels of H(2)O(2)-induced ferryl heme are produced by free met-α-subunits as compared with met-β-subunits, and no ferryl heme is detected in H(2)O(2)-treated AHSP·met-α-complex at pH values from 5.0 to 9.0 at 23 °C. Ferryl heme species were similarly not detected in AHSP·met-α Pro-30 mutants known to exhibit different rates of autoxidation and hemin loss. EPR data suggest that protein-based radicals associated with the ferryl oxidation state exist within HbA α- and β-subunits. In contrast, treatment of free α-subunits with H(2)O(2) yields much smaller radical signals, and no radicals are detected when H(2)O(2) is added to AHSP·α-complexes. AHSP binding also dramatically reduces the redox potential of α-subunits, from +40 to -78 mV in 1 m glycine buffer, pH 6.0, at 8 °C, demonstrating independently that AHSP has a much higher affinity for Fe(III) versus Fe(II) α-subunits. Hexacoordination in the AHSP·met-α complex markedly decreases the rate of the initial H(2)O(2) reaction with iron and thus provides α-subunits protection against damaging oxidative reactions.
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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.