[HTML][HTML] Reversible hexacoordination of α-Hemoglobin-stabilizing Protein (AHSP)/α-hemoglobin versus pressure: evidence for protection of the α-chains by their …

D Hamdane, C Vasseur-Godbillon… - Journal of biological …, 2007 - ASBMB
Using high hydrostatic pressure or hydrogen peroxide as perturbing agents, we demonstrate
a protective effect of the chaperone AHSP for the α-chains of Hb. High pressure induces an
irreversible aggregation of the ferrous deoxy α-chains, whereas the AHSP/α-Hb complex
shows reversible hexacoordination of the α-Hb without protein aggregation. Upon pressure
release, the relaxation kinetics of the transition from the hexacoordinated to
pentacoordinated form of α-Hb in the presence of AHSP exhibit a biphasic shape. High …