ArticleRedox biology2018
Site-directed mutagenesis of cysteine residues alters oxidative stability of fetal hemoglobin.
Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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.
The trial behind it
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
15 citing papers in PubMed, 22 citations in OpenAlex.
- Oxidative Characteristics of Turkey Hemoglobin A Containing Covalently Bound Epigallocatechin Gallate.Journal of agricultural and food chemistry · 2026Article
- Gas-Binding Studies of Class 1 Sugar Beet Phytoglobin and C86A Mutant Using Isothermal Spectral Shifts in High-Precision Microliter Assay.International journal of molecular sciences · 2025Article
- N-methylation of histidine to tune tautomeric preferences in histidine-heme coordination and enzyme-mimetic catalysis.Smart molecules : open access · 2024Article
- Factors Influencing Venous Remodeling in the Development of Varicose Veins of the Lower Limbs.International journal of molecular sciences · 2024Review
- How Nitric Oxide Hindered the Search for Hemoglobin-Based Oxygen Carriers as Human Blood Substitutes.International journal of molecular sciences · 2023Review
- Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome.Cell chemical biology · 2023Article
- Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome.bioRxiv : the preprint server for biology · 2023Article
- Structural and oxidative investigation of a recombinant high-yielding fetal hemoglobin mutant.Frontiers in molecular biosciences · 2023Article
- Oxidative Implications of Substituting a Conserved Cysteine Residue in Sugar Beet Phytoglobin BvPgb 1.2.Antioxidants (Basel, Switzerland) · 2022Article
- Introducing Negatively Charged Residues on the Surface of Fetal Hemoglobin Improves Yields inFrontiers in bioengineering and biotechnology · 2021Article
- Alterations in the Plasma and Red Blood Cell Properties in Patients with Varicose Vein: A Pilot Study.Cardiology research and practice · 2021Article
- Reactive Oxygen Species and Their Involvement in Red Blood Cell Damage in Chronic Kidney Disease.Oxidative medicine and cellular longevity · 2021Review
- Site-Specific Introduction of Negative Charges on the Protein Surface for Improving Global Functions of Recombinant Fetal Hemoglobin.Frontiers in molecular biosciences · 2021Article
- βCysteine 93 in human hemoglobin: a gateway to oxidative stability in health and disease.Laboratory investigation; a journal of technical methods and pathology · 2021Review
- Effects of α subunit substitutions on the oxidation of βCys93 and the stability of sickle cell hemoglobin.Redox report : communications in free radical research · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Redox active cysteine residues including βCys93 are part of hemoglobin's "oxidation hotspot". Irreversible oxidation of βCys93 ultimately leads to the collapse of the hemoglobin structure and release of heme. Human fetal hemoglobin (HbF), similarly to the adult hemoglobin (HbA), carries redox active γCys93 in the vicinity of the heme pocket. Site-directed mutagenesis has been used in this study to examine the impact of removal and/or addition of cysteine residues in HbF. The redox activities of the recombinant mutants were examined by determining the spontaneous autoxidation rate, the hydrogen peroxide induced ferric to ferryl oxidation rate, and irreversible oxidation of cysteine by quantitative mass spectrometry. We found that substitution of γCys93Ala resulted in oxidative instability characterized by increased oxidation rates. Moreover, the addition of a cysteine residue at α19 on the exposed surface of the α-chain altered the regular electron transfer pathway within the protein by forming an alternative oxidative site. This may also create an accessible site for di-sulfide bonding between Hb subunits. Engineering of cysteine residues at suitable locations may be useful as a tool for managing oxidation in a protein, and for Hb, a way to stave off oxidation reactions resulting in a protein structural collapse.
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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.