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Band 3 catalyzes sickle hemoglobin polymerization
Journal article   Open access   Peer reviewed

Band 3 catalyzes sickle hemoglobin polymerization

Maria A. Rotter, Haiyan Chu, Philip S. Low and Frank A. Ferrone
Biophysical chemistry, v 146(2), pp 55-59
2010
DOI: https://doi.org/10.1016/j.bpc.2009.10.004
PMID: 19880238
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://europepmc.org/articles/pmc2989409View
Accepted (AM)Open Access (License Unspecified),  Open

Abstract

Band 3 Catalysis Molecular crowding Nucleation Red cell membrane Sickle hemoglobin
We have measured homogeneous and heterogeneous nucleation rates of sickle hemoglobin (HbS) in the presence of a strongly binding deletion mutant of the cytoplasmic domain of band 3 (cdb3), a membrane protein known to form dimers and to bind 2 HbS molecules to such a dimer, and we find that it accelerated both rates by a factor of 2. A weakly binding mutant, in contrast showed no impact on nucleation rates, contrary to naïve expectations of a slight enhancement based on the molecular crowding of the solution by the mutant. We find we can explain these phenomena by a model of HbS–cdb3 interaction in which the strong binding mutant, by stabilizing an HbS dimer, catalyzes the nucleation process, while the weak mutant binds only 1 HbS molecule, effectively inactivating it and thereby compensating for the crowding of the solution by the cdb3. The catalytic behavior we observe could play a role in intracellular processes.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Chemistry, Physical
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