Mechanism of O2 Binding to Globin Proteins

This set of flashcards covers key vocabulary and concepts related to the mechanism of oxygen binding in globin proteins, particularly focusing on myoglobin and hemoglobin.

Globin Proteins

Proteins that bind oxygen, such as myoglobin and hemoglobin, crucial for oxygen storage and transport.

Heme Group

A porphyrin ring with an iron atom that binds oxygen in globin proteins.

Myoglobin

A monomeric protein that binds oxygen with high affinity and serves as an oxygen reservoir in muscle cells.

Hemoglobin

A tetrameric protein consisting of four heme groups that transports oxygen in the blood.

Allosteric Regulation

Regulation of a protein's function through conformational changes induced by ligand binding.

Kd (Dissociation Constant)

A measure of the affinity of a ligand for its binding site; lower Kd indicates higher affinity.

Cooperative Binding

A phenomenon where the binding of one molecule of ligand increases the affinity for subsequent molecules.

R State (Relaxed)

The conformation of hemoglobin when it is bound to oxygen, with high affinity.

T State (Tense)

The conformation of hemoglobin when it is not bound to oxygen, with lower affinity.

Histidine Residues

Amino acids in globin proteins that play key roles in coordinating oxygen binding through interactions with the iron atom.