Substitutions in the β subunits of sickle-cell hemoglobin improve oxidative stability and increase the delay time of sickle-cell fiber formation

After reacting with hydrogen peroxide (H(2)O(2)), sickle-cell hemoglobin (HbS, βE6V) remains longer in a highly oxidizing ferryl form (HbFe(4+)=O) and induces irreversible oxidation of “hot-spot” amino acids, including βCys-93. To control the damaging ferryl heme, here we constructed three HbS varia...

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Dettagli Bibliografici
Pubblicato in:J Biol Chem
Autori principali: Meng, Fantao, Kassa, Tigist, Strader, Michael Brad, Soman, Jayashree, Olson, John S., Alayash, Abdu I.
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Biochemistry and Molecular Biology 2019
Soggetti:
Bioenergetics
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC6422104/
https://ncbi.nlm.nih.gov/pubmed/30630954
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.006452
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