Open AccessCobalt Hemoglobin: pH Dependence of Adair Constants and the Bohr Effects
Author(s) -
SNYDER Fred W.,
CHIEN James C. W.
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb20939.x
Subject(s) - bohr effect , chemistry , cobalt , bohr model , hemoglobin , oxygen , titration , inorganic chemistry , analytical chemistry (journal) , oxygen–haemoglobin dissociation curve , chromatography , biochemistry , organic chemistry , quantum mechanics , physics
Precise oxygen equilibrium curves have been obtained for cobalt hemoglobin at pH values from 5.5 to 8.2. The Hill plots are symmetric having asymptotes with slopes of unity. At pH 7.0, cobalt hemoglobin has p 0.5 = 116 torr (15.45 kPa), p m = 117 torr (15.58 kPa) and a Hill coefficient of n = 1.72. The values of n decrease slightly with either decrease or increase of pH; the protein is almost non‐cooperative at pH ≥ 8.2. The Adair constants have been calculated with a non‐linear least‐squares program. From δIn p m /δpH a maximum of 2.5 Bohr protons was calculated at physio‐ logical pH values. The majority of alkaline Bohr protons are released after binding of the first and the third oxygen with maxima at pH 7.6 and 7.3, respectively. The acid Bohr effect was also observed with the majority of the protons taken up following the first and third oxygen bound. Smaller alkaline Bohr effects were obtained by differential titration and at higher pH than that calculated from oxygen equilibria. The discrepancy can be largely attributed to the binding of salt components to cobalt hemoglobin.