Hemocyanins

Literature References: A non-heme, oxygen carrying copper protein found in arthropods and mollusca of which keyhole-limpet hemocyanin (KLH) is an example. Dissolved in the hemolymph; not found in blood cells. Mol wt ranges from 4.5 ´ 105 to 1.3 ´ 107. One molecule of oxygen is bound by two copper atoms. The oxygenated form, oxyhemocyanin is blue, while deoxyhemocyanin is colorless. The copper can be removed reversibly to form apohemocyanin. Structure of snail, Helix pomatia, hemocyanin: J. E. Mellema, A. Klug, Nature 239, 146 (1972). The role of copper in hemocyanin: R. Lontie, L. Vanquickenborne, Met. Ions Biol. Syst. 3, 183 (1974). Reviews: K. E. van Holde, E. F. J. van Bruggen in Subunits in Biological Systems vol. 5, pt. A, S. N. Timasheff, G. D. Fasman, Eds. (Dekker, New York, 1971) pp 1-53; R. Lontie, R. Witters in Inorganic Biochemistry vol. I, G. L. Eichhorn, Ed. (Elsevier, New York, 1973) pp 344-358; E. F. J. van Bruggen, Trends Biochem. Sci. 5, 185-8 (1980). Review of respiratory function: J. Bonaventura, C. Bonaventura, Am. Zool. 20, 7-17 (1980); C. P. Magnum, ibid. 19-38.