BOHR EFFECT

Ph which is a reflection of hydrogen ion concentration changes

and has significant effect on the affinity of oxygen for
hemoglobin. This dependency on explained by the Bohr’s Effect.
This effect serves to illustrate how the hydrogen ion concentration
affects the protein structure and its function.

In the lungs oxygen combines to form oxy-hemoglobin, as a result

of the increased oxygen pressure and low hydrogen ion
concentration which translates to a high pH and thus high affinity
of hemoglobin molecules for oxygen molecules.

Low [H+]
Hb + O2 HbO2

In the tissue there exists an opposite effect that occurs which

leads to oxygen being released this usually occurs at high
hydrogen ion concentration which results in the reduced affinity
of hemoglobin molecules for oxygen molecules.

High [H+]
HbO2 Hb + O2

Why does pH affect hemoglobin affinity?

The product of metabolism in the tissue is CO2 , which is removed

by diffusion through the tissue membranes and this diffusion is
facilitated by an enzyme called carbonic anhydrase and water
yielding an important buffer carbonic acid, HCO3- The presence of
carbonic acid, carbonic anhydrase and carbon monoxide produces
a proton, the resulting proton will bind to hemoglobin, protonating
the hemoglobin molecule,

Carbonic Anhydrse
CO2 + H2O HCO3-
+ H+

H+ + Hb HbH

This proton binds to a number of points on the hemoglobin

molecule made up of several functional groups like the alpha-
amine, carboxyl and histidine (Imidazole portion) terminal groups.

Several amino acids particularly lysine (Has an amine at its

terminal end), Arginine, all these functional groups and proteins
contribute to the behavior in the micro environment of
hemoglobin.

In the environment of hemoglobin if there exists a gradient of pH,

this change will affect the structure of the hemoglobin modifying
it as a result of charge interaction, protonating hemoglobin results
in hemoglobin losing its ability to bind the oxygen.

When CO2 travels through the circulation of buffers solutions of

blood (pH 7.4) as there is an equilibrium between production of
bicarbonate, carbon dioxide and water.

HCO3- H+
CO2 + H2O
This results in the absorption of a proton, then the hemoglobin
which was initially protonated can then give up that proton and
now the oxygen has great affinity for hemoglobin because the pH
increases, hydrogen ion concentration reduces because of the
production of CO2.

Notable is the effect of lactic acid present in the muscles which

will release a considerable amount of hydrogen ions and as a
result it will increase hydrogen ion concentration causing pH to
decrease and the affinity for oxygen to decrease, and therefore
releasing oxygen from hemoglobin in the muscles, this is
important because under these conditions 10% more oxygen is
required.