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Alkaline Bohr effect of human hemoglobin Ao.

Abstract：

:Differential oxygen binding measurements obtained over the pH range 6.95 to 9.10 at 25 degrees C have allowed a detailed description of the alkaline Bohr effect of human hemoglobin Ao. Phenomenological analysis of the data in terms of the Adair equation shows that: (1) the oxygen binding curves are asymmetrical with the population of the triply oxygenated species being negligible throughout the pH range studied: (2) the shape of the oxygen binding curve is affected by pH, especially at low saturation; and (3) the maximum O2-proton linkage is -0.52 mole of proton per mole of oxygen at pH 7.4. A possible molecular mechanism of the Bohr effect is proposed within the framework of an allosteric model which accounts for the low population of triply oxygenated hemoglobin species. At least three Bohr groups are necessary for a quantitative description of the alkaline Bohr effect. Two of these groups titrate in the range of the His146 beta and Vall alpha residues, which have long been identified as the main alkaline Bohr groups, and altogether contribute 84% of the alkaline Bohr effect at physiological pH. A third ionizable group, linked to oxygenation presumably at the beta chains, is implicated and is titrated in a pH range characteristic of a surface histidyl residue.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Di Cera E,Doyle ML,Gill SJ

doi

10.1016/0022-2836(88)90545-1

subject

Has Abstract

pub_date

1988-04-05 00:00:00

pages

593-9

issue

3

eissn

0022-2836

issn

1089-8638

pii

0022-2836(88)90545-1

journal_volume

200

pub_type

杂志文章

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