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...

Descripción completa

Detalles Bibliográficos
Autores principales: Meng, Fantao, Kassa, Tigist, Strader, Michael Brad, Soman, Jayashree, Olson, John S., Alayash, Abdu I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2019
Materias:
Bioenergetics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6422104/
https://www.ncbi.nlm.nih.gov/pubmed/30630954
http://dx.doi.org/10.1074/jbc.RA118.006452

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6422104/
https://www.ncbi.nlm.nih.gov/pubmed/30630954
http://dx.doi.org/10.1074/jbc.RA118.006452

Ejemplares similares