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• W96637897 abstract "Substitutions of Asn, Glu, and Leu for Gln at the β131 position of the hemoglobin molecule result in recombinant hemoglobins (rHbs) with moderately lowered oxygen affinity and high cooperativity compared to human normal adult hemoglobin (Hb A). The mutation site affects the hydrogen bonds present at the α1β1-subunit interface between α103His and β131Gln as well as that between α122His and β35Tyr. NMR spectroscopy shows that the hydrogen bonds are indeed perturbed; in the case of rHb (β131Gln → Asn) and rHb (β131Gln → Leu), the perturbations are propagated to the other α1β1-interface H-bond involving α122His and β35Tyr. Proton exchange measurements also detect faster exchange rates for both α1β1-interface histidine side chains of the mutant rHbs in 0.1 M sodium phosphate buffer at pH 7.0 than for those of Hb A under the same conditions. In addition, the same measurements in 0.1 M Tris buffer at pH 7.0 show a much slower exchange rate for mutant rHbs and Hb A. One of the mutants, rHb (β131Gln → Asn), shows the conformational exchange of its interface histidines, and exchange rate measurements have been attempted. We have also conducted studies on the reactivity of the SH group of β93Cys (a residue located in the region of the α1β2-subunit interface) toward p-mercuribenzoate, and our results show that low-oxygen-affinity rHbs have a more reactive β93Cys than Hb A in the CO form. Our results indicate that there is communication between the α1β1- and α1β2-subunit interfaces, and a possible communication pathway for the cooperative oxygenation of Hb A that allows the α1β1-subunit interface to modulate the functional properties in conjunction with the α1β2 interface is proposed." @default.
• W96637897 created "2016-06-24" @default.
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• W96637897 date "2002-03-30" @default.
• W96637897 modified "2023-10-10" @default.
• W96637897 title "Effects of Amino Acid Substitutions at β131 on the Structure and Properties of Hemoglobin: Evidence for Communication between α₁β₁- and α₁β₂-Subunit Interfaces" @default.
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• W96637897 doi "https://doi.org/10.1021/bi011919d" @default.
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