A possible new mechanism of oxygen affinity modulation in mammalian hemoglobins
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Enthalpic partitioning of the reduced temperature sensitivity of O<inf>2</inf> binding in bovine hemoglobin
2014, Comparative Biochemistry and Physiology -Part A : Molecular and Integrative PhysiologyCitation Excerpt :In cold-tolerant mammals (including reindeer, horse and cattle) the low temperature sensitivities have been suggested to correlate with the presence of the additional Cl− binding site compared to human Hb. In contrast to human Hb, where chloride ions predominantly bind at one α-chain site (involving Val1α and Ser131α) and one β-chain site (involving Val1β and Lys82β) (O'Donnell et al., 1979; Riggs, 1988), Hbs from these species have a cluster of positively charged (His and Lys) amino acid residues at positions 8, 76 and 77 of the β-chains (Fronticelli, 1990) (Table 1), that potentially increases the endothermic contribution of Cl− release upon O2 binding. In accordance with this contention, a human Hb mutant constructed to contain ‘bovine’, β-chain amino acid substitutions including Ala76β→Lys, displayed a heightened Cl− sensitivity (Fronticelli et al., 1995) — although these substitutions did not reduce O2 affinity to the level found in bovine Hb (Baudin-Creuza et al., 2002).
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