Haemoglobin

Haemoglobin is a molecule, a protein more specifically, found in our

erythrocytes. Its primary function is to transport oxygen. Since
oxygen is not very soluble in water, an oxygen transport protein
must be used to allow oxygen to become soluble.

A haemoglobin molecule is a globular protein and is composed of

four polypeptide chains, two alpha and two beta chains. Each chain
has a tertiary structure with helical secondary structures.

As seen on the left, many amino

acids link together via
condensation reactions, causing
peptide bonds to form between
the individual molecules,
creating a polypeptide chain.
Through a reaction involving
enzymes, the chain curls into a
spiral shape, forming a helix. To
keep a fixed structure hydrogen
bonds form between hydrogen
and oxygen atoms of adjacent,
and every second or third amino
acid. Individually these forces of
attraction are weak, yet together
they are very strong and much
energy is required to break
them.

As seen on the right, the long

helix entwines itself and forms
almost a spherical structure. As
mentioned earlier, haemoglobin
consists of two alpha chains and
two beta chains joined together.
An alpha chain is 141 amino
acids long and is produced by a
gene on chromosome no.16. A
beta chain is 146 amino acids
long and is produced by a gene
on chromosome no.11.

Encompassed in each polypeptide chain is a haem group. Each

haem group can carry one oxygen molecule, and thus two oxygen
atoms. Meaning one haemoglobin protein can carry up to eight
oxygen atoms. Out of interest, because in humans the average
haemoglobin concentration is 16g/100ml, there are around
150,500,000,000,000,000,000 haemoglobin molecules in 100ml of
whole blood. Therefore, 100ml of blood can carry up to 1.2x 1021
oxygen atoms.

A haem group is another organic molecule, but much smaller than

that of a polypeptide chain. As shown above, it consists of one
central iron atom surrounded by four nitrogen atoms. Methyl, vinyl,
pyrrole rings and a propionate group in turn surround and constitute
these. The central iron atom binds to porphyrin ring, but this leaves
two free bonding sites for the iron, one on either side of the haem
plane. One of these bonding sites is joined to one of the histidines,
thus leaving the final bonding site available to reversibly bond with
oxygen.
When the structure of Haemoglobin changes shape, its affinity for
oxygen is also altered, therefore either increasing or decreasing its
affinity. When haemoglobins affinity is greater, the haemoglobin in
the blood closer to the lungs is able to bind to oxygen for transport
to regions in need of fresh oxygen. At which point, haemoglobin will
then undergo a structural change and let go of the oxygen for cells
to use.

Therefore, structurally, a haemoglobin molecule is a protein

consisting of four polypeptide chains, each containing 1 haem group
that is made up of an iron atom surrounded by various other rings
and groups.

Chlorophyll
As I was researching haemoglobin, I came across the structure of
chlorophyll:

Looking at this diagram, one can immediately see that the structure
of haemoglobin and chlorophyll, found in plants, is almost identical.
The main difference is that the magnesium in chlorophyll has
replaced the iron atom in haemoglobin. Having done some further
research, I came upon this diagram, which seems to show that
haemoglobin and chlorophyll come from the same precursor,
protoporphyrin?