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Created by: Team Chemistry - Examples.com, Last Updated: April 25, 2024


Hemoglobin is a complex compound crucial in the field of chemistry and biology, primarily responsible for transporting oxygen from the lungs to various parts of the body and then carrying carbon dioxide back to the lungs to be exhaled. This protein is found in the red blood cells and gives them their characteristic red color. Understanding hemoglobin helps us grasp how oxygen reaches our vital organs and tissues, emphasizing its significant role in sustaining life. Its structure includes iron, which binds oxygen, showcasing the intricate relationship between chemical elements and biological functions.

What is Hemoglobin?

It is an vital protein found in red blood cells that carries oxygen from the lungs to the rest of the body and transports carbon dioxide back to the lungs to be exhaled. This protein gives red blood cells their characteristic color and plays a crucial role in maintaining the body’s energy levels and overall health. Chemically it can be represented by the formula C₃₄H₃₂FeN₄O₄, . Its structure allows it to bind efficiently with oxygen, making it essential for supporting life’s metabolic processes. Understanding it helps us appreciate how our bodies utilize oxygen and manage waste gases like carbon dioxide.

Types of Hemoglobin

Hemoglobin A (HbA)

In healthy adults, Hemoglobin A constitutes about 97% of the hemoglobin. It features two alpha and two beta chains. This structure optimally transports oxygen from the lungs to various body parts and carries carbon dioxide back to the lungs for exhalation.

Hemoglobin A2 (HbA2)

Making up about 2-3% of hemoglobin in adults, Hemoglobin A2 has two alpha and two delta chains. Its presence is normal but in much smaller amounts compared to Hemoglobin A. Increased levels of HbA2 can indicate beta-thalassemia, a blood disorder.

Hemoglobin F (HbF)

In fetuses and newborn babies, Hemoglobin F predominates. It comprises two alpha chains and two gamma chains, enhancing oxygen capture from the mother’s bloodstream. After birth, the concentration of HbF significantly decreases and Hemoglobin A replaces it.

Hemoglobin S (HbS)

Hemoglobin S is a variant of hemoglobin that is associated with sickle cell disease. It arises due to a mutation in the beta chain, which causes the hemoglobin to form a sickle shape under low oxygen conditions. This abnormal shape can lead to various complications as it obstructs blood flow.

Hemoglobin C (HbC)

Hemoglobin C is another variant caused by a mutation in the beta chain. People with Hemoglobin C or Hemoglobin C trait usually do not have symptoms, though some might have a mild anemia. Hemoglobin C can affect the overall shape and function of red blood cells.

Structure of Hemoglobin


Hemoglobin is a complex protein made up of four subunits, each containing a heme group that holds an iron atom. This structure is key for its ability to bind and transport oxygen throughout the body. The four subunits are arranged in pairs: two alpha chains and two beta chains, forming a roughly spherical shape. Each iron atom in the heme groups can bind one oxygen molecule, allowing hemoglobin to efficiently pick up oxygen in the lungs and release it in tissues that need it most. This unique arrangement ensures that hemoglobin functions effectively as the body’s oxygen transporter, critical for sustaining cellular processes and overall health.

Preparation of Hemoglobin

The body naturally produces hemoglobin, specifically within the bone marrow. The synthesis involves forming globin proteins and the heme group. The translation of mRNA, which encodes the alpha and beta chains of hemoglobin, produces globin. Simultaneously, the heme group synthesis occurs through a series of chemical reactions beginning with succinyl-CoA and glycine, leading to the production of a molecule called porphyrin. This porphyrin then incorporates iron to form the complete heme group. The chemical reaction is:

Succinyl-CoA + Glycine Porphyrin + Fe Heme

Once both components are available, they combine to form the complete hemoglobin molecule, ready to transport oxygen throughout the body. This synthesis is crucial for maintaining healthy oxygen levels in our tissues and organs.

Functions of Hemoglobin


Oxygen Transport

Hemoglobin primarily functions to transport oxygen from the lungs to various tissues and organs throughout the body. In the lungs, each hemoglobin molecule can bind up to four oxygen molecules. Cells that require oxygen for energy production and metabolic processes then receive this oxygen.

Carbon Dioxide Removal

In addition to transporting oxygen, hemoglobin also critically transports carbon dioxide from tissues back to the lungs. Carbon dioxide, a metabolic waste product, binds to hemoglobin, forming carbaminohemoglobin. The lungs then expel this bound carbon dioxide through exhalation, accounting for about 20-25% of the body’s carbon dioxide.

Buffering Blood pH

Hemoglobin helps maintain the pH balance in our blood by buffering changes in acidity. When hemoglobin picks up carbon dioxide, it forms bicarbonate ions, which help neutralize pH variations. This buffering capability is vital for maintaining stable physiological conditions.

Regulation of Blood Flow

It also influences the regulation of blood flow and distribution around the body. By binding with gases like nitric oxide, hemoglobin can help relax the blood vessels, increasing blood flow and improving oxygen delivery to needy areas of the body.

Hemoglobin: Causes and Effects of Low Levels

  • Iron Deficiency: The most common cause of low hemoglobin. Iron is crucial for producing hemoglobin, and its deficiency leads to decreased production.
  • Vitamin Deficiencies: Lack of vitamins B12 or folate can impair hemoglobin production and lead to anemia.
  • Chronic Diseases: Conditions like kidney disease can affect hemoglobin production.
  • Blood Loss: Losing significant amounts of blood from surgery or injury reduces hemoglobin levels quickly.

Effects of Low Hemoglobin

  • Fatigue: Less hemoglobin means fewer oxygen-carrying red blood cells, leading to tiredness and weakness.
  • Shortness of Breath: Low hemoglobin levels make it harder for your body to meet oxygen demands, causing breathlessness.
  • Pale Skin: Hemoglobin gives skin its rosy color, so lower levels can lead to paleness.
  • Heart Problems: The heart must work harder to circulate oxygen when hemoglobin levels are low, potentially leading to heart complications.


What is a Good Hemoglobin Level?

Ideal hemoglobin levels vary: men should have 13.8 to 17.2 grams per deciliter, and women, 12.1 to 15.1 grams per deciliter.

What Are the two major components of Hemoglobin?

Hemoglobin’s major components are globin proteins and heme groups, essential for oxygen transport.

What Does Hemoglobin Bind To?

Hemoglobin binds to oxygen in the lungs and carbon dioxide in tissues, facilitating gas exchange.

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