Bioinorganic Chemistry

Hemoglobin and Myoglobin

Oxygen transfer and storage agents in the blood and
muscle tissue.
Hemoglobin transports oxygen (O2) from the lungs/gills
to tissues and muscles.
Myoglobin stores oxygen (O2) in the muscles and
tissues.
Oxygen commonly transfers from the hemoglobin to the
myoglobin for later use.

HEMOGLOBIN: COOPERATIVITY
Cooperativity
The function of hemoglobin is to bind O2 at high oxygen
pressure and carry it through the blood to needed areas (and
myoglobin for storage).
Hb + 4O2 Hb(O2)4
Hb(O2)4 + 4Mb 4Mb(O2) + Hb
As one iron binds an oxygen molecule in Hb, the molecular shape
changes to make binding of additional oxygen molecules easier. In
a similar fashion, initial removal of oxygen triggers the release of
the remaining oxygens.

HEMOGLOBIN: COOPERATIVITY
Cooperative binding of oxygen by
the four subunits of hemoglobin
means that the binding of an
oxygen molecule at one heme
group

increases

the

oxygen

affinity of the remaining heme

groups in the same hemoglobin
molecule

 The cooperative binding of

oxygen allows hemoglobin to
deliver more oxygen to the tissues
in response to relatively small
changes in the partial pressure of
oxygen.

In the lung, the concentration of

oxygen is high and hemoglobin
becomes saturated (or loaded)
with oxygen.
In
the
peripheral
tissues,
oxyhemoglobin
releases
(orunloads) much of its oxygen
for use in the tissues
5

 Saturation curve for Mb shows rapid

oxygen concentration-dependent saturation
of monomeric oxygen-binding protein.
The

Hb

curve

shows

the

sigmoidal

saturation curves for cooperative oxygen

binding.
Also indicated in the diagram are the
typical oxygen concentrations in peripheral
tissues and the lungs.
Note that whereas, myoglobin can be fully
oxygen saturated in the tissues, hemoglobin
requires much higher oxygen concentration
to become fully saturated which only occurs
in the lungs.

At low partial pressures of O2, Mb has a much greater affinity for O2.

K Mb

[Mb(O 2 )]

[Mb][O 2 ]

K Hb

[ Hb(O2 ) 4 ]

[ Hb][O2 ]2.8

It is essential that Hb's saturation curve for O 2 binding be sigmoidal, rather

than hyperbolic.

In this case, Hb is saturated at pO 2 found in the lungs, but binds O2 weakly

at pO2 found in the tissues.

This is possible due to cooperativity.

The binding of O2 at one site in Hb increases the affinity for O 2 at other sites
in the same Hb molecule.

BOHR EFFECT

The release of oxygen from hemoglobin

is enhanced when the pH is lowered or
when the hemoglobin is in the presence
of an increased partial pressure of CO2.

This result in a decreased oxygen affinity

of hemoglobin and a shift to the right in
the oxygen dissociation curve.
This change in oxygen binding is called
the Bohr effect.
Conversely, raising the pH or lowering
the concentration of CO2 results in a

greater affinity for oxygen, and a shift to

the left in the oxygen dissociation curve.

The Bohr effect

The binding power of Hb with oxygen is pH dependent --- Bohr effect
1.

During respiration, CO2 is produced. This

Red cell
plasma

diffuses into the blood plasma and into the red

blood cells.
CO2
2.

Inside the red blood cells are many molecules of

H2O

HCO3- + H+.

an enzyme called carbonic anhydrase *.

3.

It catalyses the reaction between CO2 and H2O.

CO2

4.

H2O

HCO3-

H2CO3

The resulting carbonic acid then dissociates into HCO 3- + H+.

(Both reactions are reversible).

H2CO3

5.

Haemoglobin very readily combines with

hydrogen ions forming

haemoglobinic acid.
6.

As a consequence haemoglobin releases some of the oxygen it is carrying.

7.

By removing hydrogen ions from the solution, haemoglobin helps to

maintain the pH of the blood close to neutral. It is acting as a buffer.

Hemoglobin binds H+ when it releases O2

HbO2 + H+

HbH+ + O2

At the lungs, when oxygen rebinds, the H + released is converted to carbon

dioxide and exhaled. About 40% of acid produced by the tissues is buffered in
this way by Hb

The Bohr effect

Three Oxygen Dissociation
curves illustrating the Bohr
Effect.
Increased carbon dioxide in
the blood causes a rightshift in the curves, such that
the haemoglobin more
easily unloads the oxygen it
is carrying.

Na -K Pump
+

The sodium-potassium pump actively maintains the

gradient of sodium (Na+) and potassium ions (K+) across
the membrane.
Typically, an animal cell has higher concentrations of K + and lower
concentrations of Na+ inside the cell.

uses the energy of one ATP to pump three Na+

ions out and two K+ ions in.

EXTRACELLULAR
FLUID

Na+

[Na+] high
[K+] low

Na

Na+

Na+

Na+

Na+

Na+

Na+

CYTOPLASM

[Na+] low
[K+] high

Na+

Cytoplasmic Na+ bonds to

the sodium-potassium pump

ATP

ADP

Na+ binding stimulates

phosphorylation by ATP.

Phosphorylation causes
the protein to change its
conformation, expelling Na+
to the outside.

Loss of the phosphate

restores the proteins
original conformation.

K+ is released and Na+

sites are receptive again;
the cycle repeats.

P
P

Extracellular K+ binds
to the protein, triggering
release of the phosphate
group.