[HTML][HTML] Structural basis of peroxide-mediated changes in human hemoglobin: a novel oxidative pathway
Y Jia, PW Buehler, RA Boykins, RM Venable… - Journal of Biological …, 2007 - ASBMB
Hydrogen peroxide (H 2 O 2) triggers a redox cycle between ferric and ferryl hemoglobin
(Hb) leading to the formation of a transient protein radical and a covalent hemeprotein cross-
link. Addition of H 2 O 2 to highly purified human hemoglobin (HbA 0) induced structural
changes that primarily resided within β subunits followed by the internalization of the heme
moiety within α subunits. These modifications were observed when an equal molar
concentration of H 2 O 2 was added to HbA 0 yet became more abundant with greater …
(Hb) leading to the formation of a transient protein radical and a covalent hemeprotein cross-
link. Addition of H 2 O 2 to highly purified human hemoglobin (HbA 0) induced structural
changes that primarily resided within β subunits followed by the internalization of the heme
moiety within α subunits. These modifications were observed when an equal molar
concentration of H 2 O 2 was added to HbA 0 yet became more abundant with greater …