Question

In: Chemistry

Explain why BPG, even at higher concentration, does not affect O2 binding to Hb in the...

Explain why BPG, even at higher concentration, does not affect O2 binding to Hb in the lungs?

Solutions

Expert Solution

Human blood contain a compound called 2,3-BPG (Bisphosphoglycerate). This compound has allosteric effect. There are so many allosteric regulators for haemoglobin. BPG is one of them.

This BPG molecule binds to the central part of the deoxyhaemoglobin version of haemoglobin and stabilizes it. This state is known as T-state. If oxygen is bound to the haemoglobin, the T-state loses its strain and relaxes. That is called R-state. If T-state stability increased, the affinity towards oxygen will decrease. So BPG makes haemoglobin less likely to bind oxygen in an attempt to release the strain. In T- state, haemoglobin is very unstable. So BPG is needed to stabilize it. Because BPG decreases haemoglobin’s affinity for oxygen, it is an allosteric inhibitor of haemoglobin. Without BPG, haemoglobin would be an extremely inefficient transporter of oxygen from the lungs to the tissues, releasing only about 8% of its oxygen content. However, in the presence of 2,3-BPG, more oxygen-binding sites in the haemoglobin tetramer must be filled in order to transition from the T to the R state. Higher concentrations of oxygen must be reached in order for haemoglobin to transition from the lower-affinity T-state to the higher-affinity R state. So it will not affect the oxygen binding in lungs.


Related Solutions

Why does Hb combine with O2 in the capillaries at the lungs and separate at the...
Why does Hb combine with O2 in the capillaries at the lungs and separate at the tissue capillaries
The Hb O2 binding curve provides an excellent example of the principle that living systems operate...
The Hb O2 binding curve provides an excellent example of the principle that living systems operate on the basis of weak non covalent interactions. Starting with the curve itself, explain how processes involving weak non covalent interactions within the structure of Hb are responsible for the sigmoid O2 binding curve.
A fetus obtains its O2 from the maternal circulation via the placenta. The concentration of BPG...
A fetus obtains its O2 from the maternal circulation via the placenta. The concentration of BPG is the same in adult and fetal RBC, but BPG binds more tightly to adult Hb than to fetal Hb. Explain how this facilitates the transfer of O2 to the fetus
What would happen to the O2-binding curve of hemoglobin when BPG is removed from its environment?...
What would happen to the O2-binding curve of hemoglobin when BPG is removed from its environment? A. The shape of the binding curve will not be affected. B. The sigmoid nature of the curve would diminish. C. The sigmoid nature of the curve would become more accentuated. D. Hemoglobin will not bind O2 any more.
9. Carbon monoxide (CO) binds Hb in a similar fashion to O2, but with 200-fold higher...
9. Carbon monoxide (CO) binds Hb in a similar fashion to O2, but with 200-fold higher affinity. When presented with a mixture of O2 and CO, individual heme molecules in a single tetramer may bind to either molecule. Does the presence of small amounts of CO increase, decrease, or not change the affinity of Hb for O2? Explain (a) your choice and (b) how CO binding Hb starves tissues of O2. In your answer, please consider R and T states...
Explain the Bohr effect. How does pH (and pKa) and CO2 affect the binding affinity of...
Explain the Bohr effect. How does pH (and pKa) and CO2 affect the binding affinity of oxygen to hemoglobin in the lungs and in tissues? Which of the specific amino acids in the hemoglobin molecule are involved in facilitating the interactions that affect oxygen binding affinity. How is CO2 transported from the tissues to the lungs?
1. a. why does myoglobin with its single prosthetic group, exhibit hyperbolic O2 binding curve? b....
1. a. why does myoglobin with its single prosthetic group, exhibit hyperbolic O2 binding curve? b. Describe O2 binding behavios of myoglobin in terms of pO2 and what does the term pO2 mean (significance)? c. Explain the structural basis for cooperative oxygen binding to hemoglobin.
1 a. Mutations can change hemoglobins O2 binding properties and cause disease. Explain why mutations can...
1 a. Mutations can change hemoglobins O2 binding properties and cause disease. Explain why mutations can increase or decrese the oxygen affinity and cooperativity of hemoglobin. How can the body compensate for these changes? b. Explain why O2 binding behavior of myoglobin and hemoglobin can be summed up by a single number, (the p50)?
No more than 3 sentences, but be very specific: why is myoglobin's hyperbolic O2 binding better...
No more than 3 sentences, but be very specific: why is myoglobin's hyperbolic O2 binding better suited for muscle and hemoglobin's allosteric binding better for blood?
Using the 12 graphs explain: 1) How does the initial reactant concentration affect: the initial reaction...
Using the 12 graphs explain: 1) How does the initial reactant concentration affect: the initial reaction rate? the overall reaction order? the rate constant? 2) How does the temperature affect: the initial reaction rate? the overall reaction order? the rate constant? 3) How can the instantaneous rate of reaction be determined from the graphs? 4) How can the reaction order for a specific chemical species be determined from the graphs? 5) How can the rate constant be determined from the...
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT