Haemoglobin abbreviation

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Hemoglobin Abbreviation and Function

Hemoglobin (Hb) Overview

Hemoglobin (Hb) is the iron-containing oxygen-transport metalloprotein found in the red blood cells of vertebrates and other animals. It plays a crucial role in transporting oxygen from the lungs or gills to the rest of the body.

Structure of Hemoglobin

The term "hemoglobin" is derived from the combination of "heme" and "globin." Each heme group contains an iron atom, which is essential for binding oxygen through ion-induced dipole forces. In humans, the hemoglobin molecule is composed of four globular protein subunits.

Detailed Composition

Each subunit of hemoglobin consists of a protein chain tightly associated with a non-protein heme group. The heme group includes an iron (Fe) ion held within a heterocyclic ring known as a porphyrin. The iron ion binds with four nitrogens in the center of the ring, all lying in one plane. Additionally, the iron is strongly bound to the globular protein via the imidazole ring of the F8 histidine residue below the porphyrin ring. A sixth position can reversibly bind oxygen, completing the octahedral group of six ligands. When oxygen is not bound, a weakly bonded water molecule fills the site, forming a distorted octahedron.

X-ray Analysis of Hemoglobin

Three-dimensional X-ray analysis of reduced hemoglobin has achieved a resolution of 5.5 Å, which reveals the course of the polypeptide chains and the positions of the heme groups. However, this resolution does not allow individual amino acid residues to be seen. Each subunit is composed of protein chains known as α chains and β chains.

Conclusion

Hemoglobin (Hb) is a vital protein in the blood, responsible for oxygen transport. Its structure, consisting of heme and globin components, allows it to efficiently bind and release oxygen, a process critical for the survival of vertebrates and other animals. Understanding its detailed structure and function is essential for insights into various physiological and pathological conditions.