9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily, metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name and explain the "trick" depicted by images below. In your answer, be certain to explain the effect on hemoglobin structure. 1.0r az Lys 40 *pH 7.6 Y 0.5- `pH 7.4 C terminus pH 7.2 Added proton B, His 146 B, Asp 94 6. 8 10 Fre po, (kPa)
9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily, metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name and explain the "trick" depicted by images below. In your answer, be certain to explain the effect on hemoglobin structure. 1.0r az Lys 40 *pH 7.6 Y 0.5- `pH 7.4 C terminus pH 7.2 Added proton B, His 146 B, Asp 94 6. 8 10 Fre po, (kPa)
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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Gene expression is a process by which the instructions present in deoxyribonucleic acid (DNA) are converted into useful molecules such as proteins, and functional messenger ribonucleic (mRNA) molecules in the case of non-protein-coding genes.
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Transcribed Image Text:**Question 9:**
Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily, metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name and explain the “trick” depicted by images below. In your answer, be certain to explain the effect on hemoglobin structure.
**Graph Explanation:**
The graph on the left is an oxygen-binding curve showing the relationship between the partial pressure of oxygen (pO₂) and the fractional saturation of hemoglobin (Y). It includes three curves representing different pH levels: 7.6, 7.4, and 7.2.
- At a lower pH (7.2), the curve shifts to the right, indicating hemoglobin's decreased affinity for oxygen, facilitating oxygen release.
- At a higher pH (7.6), the curve shifts to the left, showing increased oxygen affinity.
**Molecular Diagram Explanation:**
The molecular diagram on the right shows the structural interaction involved:
- The added proton (H⁺) at a lower pH affects the structure of hemoglobin.
- It shows interactions between specific amino acid residues: α2 Lys 40, C terminus, β1 His 146, and β1 Asp 94.
- The protonation of histidine (His 146) enhances its positive charge, facilitating a salt bridge with aspartate (Asp 94), stabilizing the deoxygenated form of hemoglobin and promoting oxygen release.
This mechanism is known as the Bohr effect, where increased acidity (lower pH) in tissues enhances oxygen release from hemoglobin, meeting the high metabolic demand for oxygen.
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