zenodoopen
Docking of GSH and BPG to the hemoglobin molecule in the oxy and deoxy state
<p>Oxy-Hb contains four bound GSH molecules inside the cavity, two of them at the β-β interface (sites 1 and 2) and two at the α-α chains interface (sites 3 and 4). In deoxy-Hb, two GSH molecules from the β-β subunits interface are released from the sites 1 and 2 allowing BPG to bind. Reoxygenation of Hbb is associated with release of BPG from its binding site and binding of two GSH molecules to the sites 1 and 2. The sites 3 and 4 remain occupied by GSH independent of the Hb conformation.</p>
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