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( Hemoglobin) Hemoglobin (also spelled haemoglobin and abbreviated Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red blood cells of vertebrates.[1]

In mammals, the protein makes up about 97% of the red blood cell’s dry content, and around 35% of the total content (including water). Hemoglobin transports oxygen from the lungs or gills to the rest of the body, such as to the muscles, where it releases the oxygen for cell use. It also has a variety of other roles of gas transport and effect-modulation which vary from species to species, and are quite diverse in some invertebrates.

The oxygen-carrying protein hemoglobin was discovered by Otto Funke in 1851.[2] In that year he published a series of articles in which he described growing hemoglobin crystals by successively diluting red blood cells with a solvent such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution.[3]

Hemoglobin’s reversible oxygenation was described a few years later by Felix Hoppe-Seyler.[4] In 1959 Max Perutz determined the molecular structure of hemoglobin by X-ray crystallography.[5][6] This work resulted in his sharing with John Kendrew the 1962 Nobel Prize in Chemistry.

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