When oxygen binds to a subunit of hemoglobin, the ____ will ____. (5 points) Select one: a. T conformation of hemoglobin ---- shift to the R state b. Distal histidine (His-64) ---- move away from the O2, decreasing the affinity for iron c. Distal histidine (His-64) ---- be bound to water d. R conformation of hemoglobin ---- shift to the T state e. Proximal histidine (His-93) ---- be bound to oxygen
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If hemoglobin is in its T state, which section of the protein first moves in response to oxygen binding? Explain the process. A) Distal histidine B) Proximal histidine C) The side chains located between the four subunits D) None of these answers
Madhur L.
56. The affinity of hemoglobin for oxygen increases as the pH is increased. 57. The binding of oxygen to hemoglobin is best described as cooperative. 58. CO binds better to free heme than it does to the heme in myoglobin because free heme has two binding sites for CO while heme in myoglobin has one. 59. Fetal hemoglobin has a higher affinity for oxygen than adult hemoglobin because fetal hemoglobin does not bind well to 2,3-BPG. 60. Sickle cell anemia is due to a mutation of a hydrophobic amino acid in hemoglobin to a polar amino acid.
What is the functional role of the "distal histidine"? It binds tightly to the heme iron to stabilize the complex between iron and oxygen. It stabilizes the complex between Fe2+ and dioxygen. It donates a hydrogen bond to the bound oxygen molecule to stabilize the complex between iron and oxygen. It stabilizes the oxygen complex and catalyzes the oxidation of iron to the ferric state. It improves access of carbon monoxide to the heme and inhibits oxidation of iron to the ferric state.
Adi S.
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