Haemoglobin

Front 1

Describe the structure and function of haemoglobin

Back 1

•haemoglobin helps to transport oxygen around the body

•each red blood cell contains haemoglobin which is a quaternary structure made up of 4 polypeptide chains

•each chain has a haem group which contains an iron ion and gives the blood cells it’s red colour

Front 2

What is meant by affinity for oxygen?

Back 2

Tendency to combine with oxygen

Front 3

What type of affinity does haemoglobin have for oxygen?

Back 3

High

Front 4

What is the equation for the formation of icy haemoglobin?

Back 4

He + 4o2 ➡️ hbo8

Front 5

What is partial pressure of oxygen?

Back 5

Oxygen concentration

Front 6

Describe how partial pressure of oxygen affects haemoglobin?

Back 6

Oxygen is loaded onto haemoglobin where there is high po2 (alveoli) and is unloaded in low po2 (respiring cells)

Front 7

Why is the dissociation curve an s shape?

Back 7

When haemoglobin binds with the first oxygen molecule, its shape alters in a way to make it easier for other oxygen molecules to join. When haemoglobin becomes more saturated, it becomes harder for oxygen to bind. The steepness in the middle is when it is easier for the oxygens to bind and the shallow ends at the ends are where it is harder for the oxygens to bind

Front 8

Explain the Bohr effect

Back 8

•respiring cells produce co2 increasing pco2

•increases rate of dissociation of oxygen

•curve shifts to the right meaning that less is haemoglobin is saturated with oxygen as more of it is being unloaded than loaded

Front 9

Describe haemoglobin in different organisms

Back 9

•organisms which live in environments with low po2 have haemoglobin with a higher affinity for oxygen compared to human haemoglobin so the curve is more to the left. This is because at low po2 more haemoglobin is saturated

Organism which are active have a lower affinity for oxygen because so curve is more to the right as at higher po2 there is lower saturation of oxygen because more is being unloaded