Symmetry distortion in the human hemoglobin tetramer induced by asymmetric ligation

FEBS Letters
Naoya Shibayama

Abstract

To investigate the conformational changes in human tetrameric (αβ)(2) hemoglobin upon binding of the first two ligands, we have measured the kinetics of reactions between 4,4'-dithiodipyridine and β93Cys sulfhydryl groups of four diliganded hemoglobins by using CO-bound Fe(II)-Ni(II) hybrids with and without β-β cross-linking. The data show that all the diliganded intermediates have high sulfhydryl reactivities, which are greater than or equal to that for the fully-liganded end state, especially when containing liganded α subunit(s). The results also reveal that both the asymmetrically (α1β1 and α1β2) diliganded species show similar high rates of sulfhydryl reactivity and biphasic kinetics, suggesting a new conformation but only slight functional distortion caused by asymmetric ligation.

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Citations

Mar 19, 2014·Journal of the American Chemical Society·Naoya ShibayamaSam-Yong Park

Related Concepts

4,4'-dipyridyl disulfide
Cross-Linking Reagents
Disulfides
Eryhem
Iron
Nickel
Protein Conformation
Pyridines
Hemoglobin
Ligands

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