Structure of Hemoglobin



Hemoglobin is a protein found in red blood cells (erythrocytes) that plays a crucial role in transporting oxygen throughout the body. It is composed of four subunits, each containing a heme group, which is responsible for binding oxygen.

Subunit Composition

Hemoglobin is made up of two alpha chains and two beta chains, each of which consists of approximately 141-146 amino acids. These chains are held together by various types of bonds and interactions.

Alpha Chains

The alpha chains are encoded by two genes, HBA1 and HBA2, located on chromosome 16. These chains are highly conserved and contribute to the stability and overall structure of hemoglobin.

Beta Chains

The beta chains are encoded by a single gene, HBB, located on chromosome 11. Mutations in this gene can lead to various hemoglobinopathies, such as sickle cell disease and beta-thalassemia.

Heme Group

The heme group is a prosthetic group that binds to each subunit of hemoglobin. It consists of an iron ion (Fe2+) coordinated to a porphyrin ring. The iron ion can reversibly bind to oxygen, allowing hemoglobin to transport oxygen from the lungs to the tissues.

Quaternary Structure

The four subunits of hemoglobin come together to form a quaternary structure. This structure is essential for the proper functioning of hemoglobin and its ability to bind and release oxygen.

Interactions between Subunits

The subunits of hemoglobin interact with each other through various types of bonds, including hydrogen bonds, hydrophobic interactions, and salt bridges. These interactions contribute to the stability of the quaternary structure.

Conformational Changes

Hemoglobin undergoes conformational changes upon binding to oxygen. When oxygen binds to one subunit, it induces structural changes that increase the affinity of the other subunits for oxygen. This phenomenon is known as cooperativity.

Role in Oxygen Transport

Hemoglobin’s primary function is to transport oxygen from the lungs to the tissues. The binding and release of oxygen is influenced by various factors, including partial pressure of oxygen, pH, temperature, and concentration of other molecules such as carbon dioxide and hydrogen ions.

Oxygen Binding Curve

The relationship between the partial pressure of oxygen (pO2) and the percentage of hemoglobin saturated with oxygen is described by the oxygen dissociation curve. This curve helps to understand how hemoglobin’s affinity for oxygen is affected by different physiological conditions.

Hemoglobin Variants

There are several naturally occurring variants of hemoglobin that can lead to different functional properties or pathological conditions.

Sickle Cell Hemoglobin

Sickle cell hemoglobin (HbS) is a variant caused by a point mutation in the beta chain gene. This mutation leads to the formation of abnormal hemoglobin molecules that can polymerize and cause red blood cells to assume a sickle shape. This results in various complications and symptoms in individuals with sickle cell disease.

Fetal Hemoglobin

Fetal hemoglobin (HbF) is a variant that is predominant during fetal development and gradually decreases after birth. It has a higher affinity for oxygen than adult hemoglobin (HbA) and plays a crucial role in facilitating oxygen transfer from the mother to the fetus.


Hemoglobin is a complex protein with a well-defined structure that allows it to efficiently transport oxygen. Understanding the detailed structure and function of hemoglobin is essential for comprehending various genetic disorders and developing effective therapeutic interventions.

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