Haemoglobin

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Haemoglobin

Haemoglobin (pronunciation: /ˈhiːməˌɡloʊbɪn/; also spelled hemoglobin and abbreviated Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates.

Etymology

The word "haemoglobin" is derived from the Greek words "haima" meaning "blood" and "globin" from the word "globus" meaning "ball". This is in reference to the protein's round, globular shape.

Function

Haemoglobin in blood carries oxygen from the lungs or gills to the rest of the body (i.e. the tissues) where it releases the oxygen to burn nutrients to provide energy to power the functions of the organism, and collects the resultant carbon dioxide to bring it back to the lungs.

Structure

In humans, haemoglobin is a tetramer (a protein with four subunits), which consists of two alpha and two beta subunits non-covalently bound, each made of 141 and 146 amino acid residues, respectively. This is organised with a heme group that contains an iron atom, which binds the oxygen molecule.

Related Terms

  • Erythrocytes: Also known as red blood cells, these are the most common type of blood cell and the vertebrate organism's principal means of delivering oxygen to the body tissues.
  • Heme: An iron-containing compound of the porphyrin class which forms the nonprotein part of haemoglobin and some other biological molecules.
  • Oxygen: A chemical element with symbol O and atomic number 8. It is a member of the chalcogen group on the periodic table and is a highly reactive nonmetal and oxidizing agent that readily forms compounds with most elements.

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