Concept explainers
Interpretation:
There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O2-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O2, and so the Fe atoms must be forced apart when O2 is bound.
- Is this molecule likely to show cooperative oxygen binding?
- Is this molecule likely to exhibit a Bohr Effect?
- Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue
Concept introduction:
When O2 binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.
The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.
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Biochemistry: Concepts and Connections (2nd Edition)
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