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Human hemoglobin molecule (1HGA)
Hemoglobin is the protein that provides transport of oxygen and carbon dioxide in blood. It is a complex protein that is localized in erythrocytes. There are several forms of this protein. Hemoglobin A which is found in adult humans is composed of four polypeptide chains, two alpha-chains and two beta-chains, each with a heme group containing an iron atom [1].
Ligand binding to all heme sites in hemoglobin does not happen simultaneously. For example the addition of first oxygen molecule causes conformational changes in protein that facilitate the rapid accession of the remaining oxygens. In environment with high level of carbon dioxide hemoglobin releases its bound oxygen. When the first oxygen molecule is disengaged, hemoglobin starts to change its shape, so other three oxygens are quickly released. Not only oxygen an carbon dioxide can bind to hemoglobin. This protein can also transport nitric oxide, carbon monooxide and several other inorganic compounds [2, 3]. Hemoglobin is one of the most well-studied proteins. It was discovered by a German physiologist Otto Funke in 1851, and its structure was first described in 1959 by Austrian molecular biologist Max Perutz who later received the Nobel Prize in chemistry for that work [4].
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This picture was repeatedly used in press including:
1. Liddington R., Derewenda Z., Dodson E., Hubbard R., Dodson G. «High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin.» J Mol Biol. 1992 Nov 20;228(2):551-79 2. Chan N.L., Rogers P.H., Arnone A. «Crystal structure of the S-nitroso form of liganded human hemoglobin.» Biochemistry. 1998 Nov 24;37(47):16459-64 3. Baldwin J.M. «The structure of human carbonmonoxy haemoglobin at 2.7 A resolution.» J Mol Biol. 1980 Jan 15;136(2):103-28 4. Perutz M.F., Rossmann M.G., Cullis A.F., Muirhead H., Will G., North A.C. «Structure of haemoglobin: a three-dimensional Fourier synthesis at
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