Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

8. Protein Function

Hemoglobin Cooperativity

Biochemistry

8. Protein Function

Hemoglobin Cooperativity

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Removal of the heme group from hemoglobin would result in which of the following?

Increased cooperativity between subunits

Loss of oxygen-binding capability

Stabilization of the R (relaxed) state

Enhanced affinity for carbon dioxide

Previous problemNext problem

Verified step by step guidance

Understand the role of the heme group in hemoglobin: The heme group is a prosthetic group containing an iron ion (Fe²⁺) that binds oxygen molecules. It is essential for hemoglobin's ability to transport oxygen in the blood.

Recognize the structural importance of the heme group: Hemoglobin is a tetrameric protein with four subunits, each containing a heme group. The heme group is directly responsible for oxygen binding, and its removal would disrupt this function.

Analyze the concept of cooperativity: Hemoglobin exhibits cooperative binding, meaning the binding of oxygen to one subunit increases the affinity of the remaining subunits for oxygen. This property depends on the presence of the heme group and the conformational changes it induces.

Evaluate the impact of heme removal on oxygen binding: Without the heme group, hemoglobin loses its ability to bind oxygen, as the iron ion in the heme is the site of oxygen attachment. This would also eliminate cooperativity between subunits.

Consider the effects on other states and molecules: The removal of the heme group would destabilize the R (relaxed) state, which is the high-affinity state for oxygen binding. Additionally, hemoglobin's interaction with carbon dioxide would not be enhanced, as this process involves different binding sites and mechanisms.