Indefinite noncooperative self-association of chicken deoxy hemoglobin D

Proteins
Mitra S Rana, Austen F Riggs

Abstract

The minor tetrameric hemoglobin (Hb), Hb D, of chicken red blood cells self-associates upon deoxygenation. This self-association enhances the cooperativity of oxygen binding. The maximal Hill coefficient is greater than 4 at high Hb concentrations. Previous measurements at low Hb concentrations were consistent with a monomer-to-dimer equilibrium and an association constant of ∼1.3-1.6 × 10(4) M(-1). Here, the Hb tetramer is considered as the monomer. However, new results indicate that the association extends beyond the dimer. We show by combination of Hb oligomer modeling and sedimentation velocity analyses that the data can be well described by an indefinite noncooperative or isodesmic association model. In this model, the deoxy Hb D associates noncooperatively to give a linear oligomeric chain with an equilibrium association constant of 1.42 × 10(4) M(-1) at 20°C for each step. The data are also well described by a monomer-dimer-tetramer equilibrium model with monomer-to-dimer and dimer-to-tetramer association constants of 1.87 and 1.03 × 10(4) M(-1) at 20°C, respectively. A hybrid recombinant Hb D was prepared with recombinant α(D)-globin and native β-globin to give a Hb D tetramer (α(2)(D)β(2)). This rHb D undergoes decreas...Continue Reading

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Citations

Sep 11, 2012·The Journal of Biological Chemistry·Michael T GrispoJay F Storz
Mar 1, 2012·Journal of Molecular Biology·Shuo YangGeoffrey J Howlett
Dec 17, 2014·Molecular Biology and Evolution·Juan C OpazoJay F Storz
May 26, 2016·The EMBO Journal·Melissa R MarzahnTanja Mittag
Sep 8, 2017·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Asbjørn G PetersenAngela Fago

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