Haemoglobin

Haemoglobin

Oxygen carrier protein in our red blood cells.

Chemistry

Keywords

haemoglobin, blood, proteid, complex protein, red blood cell, oxygen binding, oxygen transport, protein, four subunits, globular, iron-containing, metalloprotein, porphyrin ring, conjugated double bond, anaemia, myoglobin, anemia, biochemistry, chemistry, biology

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Haemoglobin

Haemoglobin

Properties

Haemoglobin is a conjugated protein which carries oxygen in our blood. It consists of four subunits, the connections between these forms the quaternary structure of the molecule. The subunits are similar to the protein myoglobin. Within the subunits, the protein part is attached to a red haem containing iron.

A porphyrin ring and a Fe-II ion form the basis of the haem. The porphyrin ring is formed by four pyrrole rings linked together by conjugated double bonds. The haem is linked to the protein chain by the Fe-II ion. Coordinative bonds make it possible for the oxygen molecule to attach to the iron ion.

The function of haemoglobin in vertebrates is to bind oxygen in the respiratory organ and deliver it to the tissues. If carbon-monoxide enters the blood, it attaches to haemoglobin more easily than oxygen, thus preventing oxygen transport. It may thus result in cell death.

Occurrence

The haemoglobin level of blood in adults is about 140 g/l for women and about 160 g/l for men. Depending on body size, blood volume, gender and other factors, there is about 700-900 grams of haemoglobin in the body.

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