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each a-ß pair are held together by disulfide bonds, these dimers are held together by hydrogen bonds and electrostatic interactions. oxygen binds directly to the proximal histidine. mutations that decrease hemoglobin's p50 (Kd) for BPG shift the oxygen dissociation curve to the right. the R state predominates when the partial pressure of oxygen is high. iron is kept in the +2 oxidation state by met-hemoglobin reductase. high proton concentrations increase the proportion of hemoglobin in the T state.

each a-ß pair are held together by disulfide bonds, these dimers are held together by hydrogen bonds and electrostatic interactions. oxygen binds directly to the proximal histidine. mutations that decrease hemoglobin's p50 (Kd) for BPG shift the oxygen dissociation curve to the right. the R state predominates when the partial pressure of oxygen is high. iron is kept in the +2 oxidation state by met-hemoglobin reductase. high proton concentrations increase the proportion of hemoglobin in the T state.

Biochemistry
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
Section: Chapter Questions
Problem 1P
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Check all of the following that applied for hemoglobin

**Key Concepts in Hemoglobin Structure and Function** 1. **Hemoglobin Structure** - Each α-β pair is held together by disulfide bonds; these dimers are further stabilized by hydrogen bonds and electrostatic interactions. 2. **Oxygen Binding** - Oxygen binds directly to the proximal histidine residue within the hemoglobin molecule. 3. **Effects of Mutations** - Mutations that decrease hemoglobin’s p50 (Kd) for BPG will shift the oxygen dissociation curve to the right, indicating a decreased affinity for oxygen. 4. **Hemoglobin States** - The R state of hemoglobin predominates when the partial pressure of oxygen is high, indicating high oxygen affinity. 5. **Iron Oxidation State** - Iron is maintained in the +2 oxidation state by the enzyme met-hemoglobin reductase, essential for oxygen binding. 6. **Proton Concentration** - High proton concentrations (low pH) increase the proportion of hemoglobin in the T state, indicating lower oxygen affinity. Understanding these concepts is essential for comprehending how hemoglobin functions in oxygen transport and release in the body.
Transcribed Image Text:**Key Concepts in Hemoglobin Structure and Function** 1. **Hemoglobin Structure** - Each α-β pair is held together by disulfide bonds; these dimers are further stabilized by hydrogen bonds and electrostatic interactions. 2. **Oxygen Binding** - Oxygen binds directly to the proximal histidine residue within the hemoglobin molecule. 3. **Effects of Mutations** - Mutations that decrease hemoglobin’s p50 (Kd) for BPG will shift the oxygen dissociation curve to the right, indicating a decreased affinity for oxygen. 4. **Hemoglobin States** - The R state of hemoglobin predominates when the partial pressure of oxygen is high, indicating high oxygen affinity. 5. **Iron Oxidation State** - Iron is maintained in the +2 oxidation state by the enzyme met-hemoglobin reductase, essential for oxygen binding. 6. **Proton Concentration** - High proton concentrations (low pH) increase the proportion of hemoglobin in the T state, indicating lower oxygen affinity. Understanding these concepts is essential for comprehending how hemoglobin functions in oxygen transport and release in the body.
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