Hemoglobin Structure and Function

The video discusses the structure and functions of hemoglobin, a protein in red blood cells. Hemoglobin is composed of globin chains and heme groups, with iron playing a crucial role in oxygen transport. The video explains the coordination of iron within the heme structure and the attachment of heme to globin chains. It also covers the functions of hemoglobin, including oxygen and carbon dioxide transport and its role as an intracellular buffer.

What is the primary function of hemoglobin in red blood cells?

• To store energy

• To fight infections

• To transport oxygen and carbon dioxide

• To digest nutrients

What is the non-protein part of hemoglobin called?

• Globin

• Heme

• Albumin

• Myoglobin

How many pyrrole rings are present in the protoporphyrin structure?

• Four

• Three

• Five

• Two

How many coordination bonds does iron form in the heme structure?

• Seven

• Six

• Five

• Four

How many polypeptide chains make up the globin part of hemoglobin?

• Two

• Three

• Five

• Four

What type of bonds stabilize the attachment of heme to globin?

• Ionic bonds

• Covalent bonds

• Non-covalent bonds

• Metallic bonds

Which amino acid residue is involved in the proximal attachment to iron in hemoglobin?

• Lysine

• Serine

• Arginine

• Histidine

What is the role of the hydrophobic pocket in hemoglobin?

• To store energy

• To oxidize iron

• To protect the iron from oxidation

• To bind carbon dioxide

What is the main function of hemoglobin in maintaining acid-base balance?

• It acts as an enzyme

• It stores oxygen

• It acts as an intracellular buffer

• It transports nutrients

Which form of iron binds to oxygen in hemoglobin?

• Oxidized

• Elemental

• Ferrous

• Ferric