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Hemoglobin is the oxygen carrier in the blood of most vertebrates. 3 bound 0₂. Po, 100 mm Hg. most likely to bind oxygen molecules 1 bound 0₂. Po₂ = 100 mm Hg B chains Ⓡ a chains hemoglobin How is hemoglobin's affinity for oxygen affected by the presence or absence of oxygen? Rank hemoglobin molecules with the described conditions from most likely to bind oxygen molecules to most likely to release oxygen molecules. (For help approaching this problem, open Hint 1.) ► View Available Hint(s) iron heme From Biology by Campbell and Reece ©2008 Pearson Education, Inc. 3 bound 0₂. Po₂ = 40 mm Hg 1 bound 0₂. Po₂ = 40 mm Hg Reset Help most likely to release oxygen molecules

Hemoglobin is the oxygen carrier in the blood of most vertebrates. 3 bound 0₂. Po, 100 mm Hg. most likely to bind oxygen molecules 1 bound 0₂. Po₂ = 100 mm Hg B chains Ⓡ a chains hemoglobin How is hemoglobin's affinity for oxygen affected by the presence or absence of oxygen? Rank hemoglobin molecules with the described conditions from most likely to bind oxygen molecules to most likely to release oxygen molecules. (For help approaching this problem, open Hint 1.) ► View Available Hint(s) iron heme From Biology by Campbell and Reece ©2008 Pearson Education, Inc. 3 bound 0₂. Po₂ = 40 mm Hg 1 bound 0₂. Po₂ = 40 mm Hg Reset Help most likely to release oxygen molecules

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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7L.4.2

**Hemoglobin and Oxygen Affinity** Hemoglobin is the oxygen carrier in the blood of most vertebrates. This lesson explores how hemoglobin’s affinity for oxygen is affected by the presence or absence of oxygen molecules. **Diagram Explanation:** The image displays a 3D structural model of hemoglobin, labeled with α chains and β chains, as well as iron heme groups. This model highlights the complex structure that allows hemoglobin to bind and release oxygen. **Interactive Activity:** You are asked to rank hemoglobin molecules under different conditions based on their likelihood to bind or release oxygen molecules. **Conditions to Rank:** 1. **3 bound O₂; P₀₂ = 100 mm Hg** 2. **1 bound O₂; P₀₂ = 100 mm Hg** 3. **3 bound O₂; P₀₂ = 40 mm Hg** 4. **1 bound O₂; P₀₂ = 40 mm Hg** **Task:** Arrange these conditions from "most likely to bind oxygen molecules" to "most likely to release oxygen molecules." This exercise helps understand how oxygen pressure (P₀₂) and the number of already bound oxygen molecules influence hemoglobin's affinity. **Hints and Assistance:** Hints are available to assist you, and you can reset or seek help as needed during the activity.
Transcribed Image Text:**Hemoglobin and Oxygen Affinity** Hemoglobin is the oxygen carrier in the blood of most vertebrates. This lesson explores how hemoglobin’s affinity for oxygen is affected by the presence or absence of oxygen molecules. **Diagram Explanation:** The image displays a 3D structural model of hemoglobin, labeled with α chains and β chains, as well as iron heme groups. This model highlights the complex structure that allows hemoglobin to bind and release oxygen. **Interactive Activity:** You are asked to rank hemoglobin molecules under different conditions based on their likelihood to bind or release oxygen molecules. **Conditions to Rank:** 1. **3 bound O₂; P₀₂ = 100 mm Hg** 2. **1 bound O₂; P₀₂ = 100 mm Hg** 3. **3 bound O₂; P₀₂ = 40 mm Hg** 4. **1 bound O₂; P₀₂ = 40 mm Hg** **Task:** Arrange these conditions from "most likely to bind oxygen molecules" to "most likely to release oxygen molecules." This exercise helps understand how oxygen pressure (P₀₂) and the number of already bound oxygen molecules influence hemoglobin's affinity. **Hints and Assistance:** Hints are available to assist you, and you can reset or seek help as needed during the activity.
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