Abstract
The relatively low solubility of oxygen in water has led, in the animal kingdom, to the development of oxygen carriers which increase the O2capacity of the blood between one and two orders of magnitude and thus provide the basis for continuous high activity. There are three types of such carriers which bind oxygen by different principles: (i) The hemoglobins, in which one Fe(II) is bound by a protoporphyrin plus one histidine residue of the globin. This has proved to be the most successful invention which occurs throughout the animal kingdom, (ii) The hemerythrins where two Fe(II) atoms bind one O2, being themselves complexes by members of the polypeptide chain; the hemerythrins are restricted to a small number of invertebrate animals, (iii) The hemocyanins, in which the active site is a pair of Cu(I) atoms which are also bind directly to the polypeptide chain; there is no heme. While hemoglobins are either intra- or extracellular, hemerythrins are exclusively intracellular and hemocyanins exclusively extracellular.
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Linzen, B., Schartau, W., Schneider, HJ. (1985). Primary Structure of Arthropod Hemocyanins. In: Lamy, J., Truchot, JP., Gilles, R. (eds) Respiratory Pigments in Animals. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70616-5_5
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DOI: https://doi.org/10.1007/978-3-642-70616-5_5
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