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Functional Changes in the Family of Type 3 Copper Proteins During Evolution
Author(s) -
Jaenicke Elmar,
Decker Heinz
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300714
Subject(s) - hemocyanin , copper protein , hydroxylation , melanin , tyrosinase , oxygen transport , copper , hemolymph , chemistry , biochemistry , melanosome , biology , oxygen , enzyme , genetics , organic chemistry , antigen
Blue blood, brown melanin: Two very different proteins share a type 3 copper active site. Tyrosinases catalyze the hydroxylation and oxidation of phenols, which results in the formation of the brown pigment melanin. Hemocyanins, on the other hand, are the oxygen‐transport proteins in the hemolymph of truly blue‐blooded animals such as spiders, scorpions, crabs, and octopus. Both proteins are closely related by evolution. But why is a hemocyanin not a tyrosinase and vice versa? What is the origin of cooperativity in these proteins? We review and discuss the structural and functional changes that took place in the evolution of type 3 copper proteins.