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The cooperative binding Of O2 in hemoglobin is due to:
- a)A decrease in size of iron followed by changes in the proton conformation.
- b)An increase in size of iron fo llowed by changes in the proton conformat ion.
- c)A decrease in size of iron that is not accompanied by the protein comformational changes.
- d)An increase in size of iron that is not accompanied by the protein comformational changes.
Correct answer is option 'A'. Can you explain this answer?
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The cooperative binding Of O2 in hemoglobin is due to:a)A decrease in ...
Hemoglobin exhibits what we call cooperative binding, as oxygen binding increases the affinity of hemoglobin for more oxygen. Increased affinity is caused by a conformational change, or a structural change in the hemoglobin molecule.
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The cooperative binding Of O2 in hemoglobin is due to:a)A decrease in ...
Explanation:
Hemoglobin is a protein found in red blood cells that binds oxygen and transports it throughout the body. The cooperative binding of O2 in hemoglobin is due to several factors, including the size of the iron atom in the heme group and changes in the protein conformation.
Size of Iron:
The iron atom in the heme group of hemoglobin is in the ferrous (Fe2+) state and is coordinated by a nitrogen atom in the heme ring and four nitrogen atoms from the protein. When oxygen binds to the iron atom, it changes from the ferrous state to the ferric (Fe3+) state, causing a decrease in the size of the iron atom. This decrease in size is due to the loss of an electron, which causes the iron atom to contract.
Protein Conformation:
The binding of oxygen to one subunit of hemoglobin causes conformational changes in the protein that facilitate the binding of oxygen to the other subunits. When oxygen binds to the iron atom in one subunit, it causes a shift in the position of the heme group and a rotation of the protein subunits. This rotation exposes a new binding site for oxygen in the other subunits, making it easier for oxygen to bind to those subunits.
Cooperative Binding:
The combination of the decrease in size of the iron atom and the protein conformational changes result in cooperative binding of oxygen to hemoglobin. Once one oxygen molecule binds to hemoglobin, it makes it easier for subsequent molecules to bind due to the conformational changes in the protein. This means that as the oxygen concentration increases, more and more oxygen molecules will bind to hemoglobin until all of the binding sites are occupied.
Conclusion:
Therefore, the cooperative binding of O2 in hemoglobin is due to a decrease in size of iron followed by changes in the protein conformation. This allows for efficient transport of oxygen throughout the body.
Hemoglobin is a protein found in red blood cells that binds oxygen and transports it throughout the body. The cooperative binding of O2 in hemoglobin is due to several factors, including the size of the iron atom in the heme group and changes in the protein conformation.
Size of Iron:
The iron atom in the heme group of hemoglobin is in the ferrous (Fe2+) state and is coordinated by a nitrogen atom in the heme ring and four nitrogen atoms from the protein. When oxygen binds to the iron atom, it changes from the ferrous state to the ferric (Fe3+) state, causing a decrease in the size of the iron atom. This decrease in size is due to the loss of an electron, which causes the iron atom to contract.
Protein Conformation:
The binding of oxygen to one subunit of hemoglobin causes conformational changes in the protein that facilitate the binding of oxygen to the other subunits. When oxygen binds to the iron atom in one subunit, it causes a shift in the position of the heme group and a rotation of the protein subunits. This rotation exposes a new binding site for oxygen in the other subunits, making it easier for oxygen to bind to those subunits.
Cooperative Binding:
The combination of the decrease in size of the iron atom and the protein conformational changes result in cooperative binding of oxygen to hemoglobin. Once one oxygen molecule binds to hemoglobin, it makes it easier for subsequent molecules to bind due to the conformational changes in the protein. This means that as the oxygen concentration increases, more and more oxygen molecules will bind to hemoglobin until all of the binding sites are occupied.
Conclusion:
Therefore, the cooperative binding of O2 in hemoglobin is due to a decrease in size of iron followed by changes in the protein conformation. This allows for efficient transport of oxygen throughout the body.
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The cooperative binding Of O2 in hemoglobin is due to:a)A decrease in size of iron followed by changes in the proton conformation.b)An increase in size of iron fo llowed by changes in the proton conformat ion.c)A decrease in size of iron that is not accompanied by the protein comformational changes.d)An increase in size of iron that is not accompanied by the protein comformational changes.Correct answer is option 'A'. Can you explain this answer?
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