How does carbon monoxide interact with hemoglobin?

Carbon monoxide interacts with hemoglobin by binding to it with an affinity approximately 200 times greater than that of oxygen. This strong binding creates a stable complex, preventing hemoglobin from effectively carrying oxygen throughout the body, which can lead to hypoxia. When carbon monoxide is inhaled, it competes with oxygen for the binding sites on hemoglobin, thereby significantly impairing oxygen delivery to tissues. This is a critical consideration in cases of carbon monoxide poisoning, as the body's ability to transport oxygen is severely compromised, eliciting urgent needs for medical intervention.

The other options fail to accurately reflect the dynamics of carbon monoxide's interaction with hemoglobin. For instance, stating that it has a weaker binding affinity than oxygen contradicts established knowledge of its binding characteristics. Similarly, the notion that it has no interaction with hemoglobin overlooks the toxic impact it has, while the idea that it displaces oxygen without binding inaccurately describes the mechanism of action, as carbon monoxide specifically binds and does not simply displace oxygen.