What is the significance of the structural changes occurring at the subunit interface of haemoglobin upon oxygen binding?
Understand the Problem
The question is asking about the implications of structural changes at the subunit interface of haemoglobin when it binds oxygen, particularly focusing on how these changes relate to its functionality as an allosteric protein.
Answer
Structural changes in hemoglobin upon oxygen binding enhance cooperativity, facilitating further oxygen binding.
The structural changes in hemoglobin upon oxygen binding involve a shift in the heme group's iron atom into the plane of the heme, facilitating the binding of additional oxygen molecules. This alteration at the subunit interface enhances oxygen binding cooperativity, making it easier for subsequent oxygen molecules to bind.
Answer for screen readers
The structural changes in hemoglobin upon oxygen binding involve a shift in the heme group's iron atom into the plane of the heme, facilitating the binding of additional oxygen molecules. This alteration at the subunit interface enhances oxygen binding cooperativity, making it easier for subsequent oxygen molecules to bind.
More Information
When oxygen binds to one of the heme groups, the iron is pulled into the plane of the heme, prompting a structural shift. This change propagates through the protein, enhancing its ability to bind more oxygen. This mechanism is an example of allosteric regulation, where the binding of one molecule influences the binding of more molecules.
Tips
Misunderstanding the role of iron movement within the heme group can lead to errors in explaining hemoglobin's oxygen-binding cooperativity.
Sources
- Hemoglobin: Structure, Function and Allostery - PMC - pmc.ncbi.nlm.nih.gov
- Structural origin of cooperativity in human hemoglobin - pmc.ncbi.nlm.nih.gov
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