Question

What kind of Oxygen-Dissociation curve do you expect when carbon monoxide attaches to hemoglobin molecules ?

Why do we observe this change from a normal oxygen dissociation curve ?

And why is this change hazardous ?
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Answer 1

Answer:

...

The graph will bend towards the left...

Explanation:

...

The dissociation curve also undergoes a leftward shift in carbon monoxide poisoning. CO has a 240-fold greater affinity for hemoglobin than oxygen and will displace oxygen. ... Despite a greater proportion of saturated hemoglobin molecules, total O2 content is decreased because of the high affinity of CO for hemoglobin...

Answer 2

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After the carbon monoxide has selectively bound to haemoglobin the oxygen-haemoglobin dissociation curve of the remaining oxyhaemoglobin shifts to the left, reducing oxygen release (Figure 1). The affinity of carbon monoxide for myoglobin is even greater than for haemoglobin1.

Binding of one CO molecule to hemoglobin increases the affinity of the other binding spots for oxygen, leading to a left shift in the dissociation curve. This shift prevents oxygen unloading in peripheral tissue and therefore the oxygen concentration of the tissue is much lower than normal.

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