UPSC MainsZOOLOGY-PAPER-II201120 Marks
Q7.

Give the chemical composition of human haemoglobin and discuss its role in O₂/CO₂ transport during various physiological states.

How to Approach

This question requires a detailed understanding of hemoglobin's structure and function. The answer should begin with the chemical composition of hemoglobin, detailing its protein and heme components. Subsequently, it should elaborate on its role in oxygen and carbon dioxide transport, differentiating between the physiological states of oxygen-rich and oxygen-poor environments, and how hemoglobin's affinity for these gases changes accordingly (Bohr effect, Haldane effect). A structured approach, dividing the answer into sections for composition, oxygen transport, and carbon dioxide transport, will be effective.

Model Answer

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Introduction

Hemoglobin, a crucial protein found in red blood cells, is responsible for the efficient transport of oxygen from the lungs to the tissues and carbon dioxide from the tissues to the lungs. Its remarkable ability to bind and release these gases is fundamental to sustaining life. The molecule’s structure is intricately linked to its function, and its behavior is modulated by various physiological factors. Understanding the chemical composition of hemoglobin and its dynamic role in gas exchange under different physiological conditions is vital for comprehending respiratory physiology. This answer will detail the composition of hemoglobin and its role in O₂/CO₂ transport during various physiological states.

Chemical Composition of Human Hemoglobin

Hemoglobin (Hb) is a globular protein belonging to the globin family. It’s a tetrameric protein, meaning it consists of four subunits. Each subunit is composed of:

  • Globulin Chain: There are different types of globin chains – alpha (α), beta (β), gamma (γ), and delta (δ). Adult hemoglobin (HbA) primarily consists of two alpha and two beta chains (α₂β₂). Fetal hemoglobin (HbF) has two alpha and two gamma chains (α₂γ₂).
  • Heme Group: Each globin chain is associated with one heme group. The heme group is a porphyrin ring complex with a central iron (Fe²⁺) atom. This iron atom is the site where oxygen binds.

The complete chemical formula for hemoglobin is C1188H1500N812O468S8Fe4. The molecular weight is approximately 64,500 Daltons.

Role in Oxygen (O₂) Transport

Hemoglobin’s primary function is oxygen transport. The process can be described as follows:

  • Oxygenation in the Lungs: In the lungs, where the partial pressure of oxygen (PO₂) is high, oxygen diffuses into the red blood cells and binds to the iron atom in the heme group of hemoglobin. This forms oxyhemoglobin (HbO₂). The binding of the first oxygen molecule increases the affinity of hemoglobin for subsequent oxygen molecules – this is known as cooperative binding.
  • Oxygen Delivery to Tissues: As blood circulates to tissues with lower PO₂, oxyhemoglobin releases oxygen. The rate of oxygen release is influenced by several factors:
    • Partial Pressure of Oxygen (PO₂): Lower PO₂ promotes oxygen dissociation.
    • Partial Pressure of Carbon Dioxide (PCO₂): Higher PCO₂ promotes oxygen dissociation (Bohr Effect).
    • pH: Lower pH (more acidic) promotes oxygen dissociation (Bohr Effect).
    • Temperature: Higher temperature promotes oxygen dissociation.
    • 2,3-Bisphosphoglycerate (2,3-BPG): Increased levels of 2,3-BPG decrease hemoglobin’s affinity for oxygen, promoting oxygen release.

Role in Carbon Dioxide (CO₂) Transport

Hemoglobin also plays a significant role in carbon dioxide transport, although not by directly binding CO₂ to the iron atom. CO₂ is transported in three main ways:

  • Dissolved CO₂: About 7-10% of CO₂ is dissolved in plasma.
  • Bicarbonate Ions (HCO₃⁻): About 70% of CO₂ is converted to bicarbonate ions within red blood cells, catalyzed by the enzyme carbonic anhydrase. This reaction is: CO₂ + H₂O ⇌ H₂CO₃ ⇌ H⁺ + HCO₃⁻.
  • Carbaminohemoglobin: About 20-23% of CO₂ binds to the globin portion of hemoglobin, forming carbaminohemoglobin (HbCO₂). This binding is reversible and is favored in tissues with high PCO₂ (Haldane Effect).

The Haldane Effect describes how oxygen dissociation promotes CO₂ binding to hemoglobin, and conversely, CO₂ binding reduces hemoglobin’s affinity for oxygen. This reciprocal relationship is crucial for efficient gas exchange.

Physiological States and Hemoglobin’s Role

Physiological State PO₂ PCO₂ pH Hemoglobin’s Affinity for O₂ Hemoglobin’s Affinity for CO₂
Lungs (Oxygenated Blood) High Low High High Low
Actively Metabolizing Tissues Low High Low Low High

Conclusion

In conclusion, hemoglobin’s chemical composition, particularly the presence of iron within the heme group, is fundamental to its ability to reversibly bind oxygen and carbon dioxide. Its role in gas transport is dynamically regulated by physiological factors like PO₂, PCO₂, pH, temperature, and 2,3-BPG, as exemplified by the Bohr and Haldane effects. Understanding these intricate mechanisms is crucial for comprehending respiratory physiology and addressing conditions affecting oxygen delivery and carbon dioxide removal. Further research into hemoglobinopathies and their impact on oxygen transport continues to be a vital area of study.

Answer Length

This is a comprehensive model answer for learning purposes and may exceed the word limit. In the exam, always adhere to the prescribed word count.

Additional Resources

Key Definitions

Bohr Effect
The Bohr effect describes the decrease in hemoglobin’s affinity for oxygen when the pH decreases or carbon dioxide concentration increases.
Haldane Effect
The Haldane effect describes the ability of oxygen to displace carbon dioxide from hemoglobin, enhancing carbon dioxide transport in the blood.

Key Statistics

Approximately 5 million red blood cells per microliter of blood contain hemoglobin. (Source: Widmaier, E. P., Raff, H., & Strang, K. T. (2016). Vander's human physiology: The mechanisms of body function. McGraw-Hill Education.)

Source: Widmaier et al., 2016

Approximately 8% of the US population carries the sickle cell trait (HbAS). (Source: CDC, 2023 - knowledge cutoff)

Source: CDC, 2023

Examples

High Altitude Adaptation

Individuals living at high altitudes exhibit increased levels of 2,3-BPG in their red blood cells. This adaptation reduces hemoglobin’s affinity for oxygen, facilitating oxygen delivery to tissues in the hypoxic environment.

Frequently Asked Questions

What is the difference between oxyhemoglobin and deoxyhemoglobin?

Oxyhemoglobin (HbO₂) is hemoglobin bound to oxygen, while deoxyhemoglobin is hemoglobin without oxygen. Deoxyhemoglobin has a slightly different conformation and color than oxyhemoglobin.

Topics Covered

BiologyPhysiologyBloodRespirationGas Exchange