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Ch. 17 Blood
Chapter 16, Problem 22

Discuss hemoglobin relative to its chemical structure, its function, and the color changes it undergoes during loading and unloading of oxygen.

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Hemoglobin is a protein found in red blood cells, composed of four polypeptide chains, each with an iron-containing heme group that can bind to oxygen.
The primary function of hemoglobin is to transport oxygen from the lungs to the tissues and facilitate the return of carbon dioxide from the tissues to the lungs.
When hemoglobin binds to oxygen in the lungs, it forms oxyhemoglobin, which is bright red in color due to the oxygenation of the iron in the heme group.
As hemoglobin releases oxygen to the tissues, it becomes deoxyhemoglobin, which is darker red or bluish in color, reflecting the reduced state of the iron.
The color change in hemoglobin during oxygen loading and unloading is due to the conformational changes in the protein structure, affecting the light absorption properties of the heme group.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Chemical Structure of Hemoglobin

Hemoglobin is a globular protein composed of four polypeptide chains, each containing a heme group that binds oxygen. The heme group consists of an iron ion at its center, which is crucial for oxygen binding. The quaternary structure of hemoglobin allows for cooperative binding, meaning that the binding of one oxygen molecule increases the affinity for additional oxygen molecules.
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Function of Hemoglobin

The primary function of hemoglobin is to transport oxygen from the lungs to the tissues and facilitate the return of carbon dioxide from the tissues back to the lungs. Hemoglobin's ability to bind oxygen is influenced by factors such as pH and carbon dioxide concentration, which are described by the Bohr effect. This ensures efficient oxygen delivery where it is most needed in the body.
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Color Changes During Oxygen Loading and Unloading

Hemoglobin exhibits distinct color changes based on its oxygenation state. When oxygen binds to hemoglobin, it transforms from a dark red color (deoxyhemoglobin) to a bright red color (oxyhemoglobin). This color change is due to alterations in the electronic structure of the heme group, which affects how light is absorbed and reflected, providing a visual indicator of oxygen saturation in the blood.
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