Abstract
Hemocyanins and Invertebrate Evolution
Highlights
Each copper is ligated by three histidine residues, as shown in Fig. 1, and lies within a 4␣-helix bundle reminiscent of hemerythrin or perhaps even the globin fold [12]
In some other molluscs dimers or even higher oligomers of these decamers can be found. Such molecules are truly immense; the structure shown in Fig. 2C has a molecular mass of about 9 ϫ 106 Da and contains 160 oxygen-binding sites! Sequence analysis [13, 14] has revealed that the functional units within a molluscan hemocyanin monomer are quite similar, with 40 –50% identity
X-ray diffraction studies have shown that octopus hemocyanin [6], two arthropod hemocyanins [5, 12], and catechol oxidase [15] exhibit remarkable similarity in the spatial arrangement of the six histidine ligands that hold the copper atoms
Summary
From the ‡Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331-7305 and ʈInstitute for Molecular Biophysics, University of Mainz, D55128 Mainz, Germany. This conservation lies in the three-dimensional structure rather than in the linear sequences. 18 and 19, for example), whereas the molluscan hemocyanins resemble more closely that group of enzymes known as tyrosinases [20] and catechol oxidases [15] Structural comparison of sweet potato catechol oxidase and the hemocyanin-binding domain from octopus reveals a specific similarity with respect to an unusual Cys-His thioether bridge, which holds one of the copper-binding histidines in the proper orientation The fact that both kinds of hemocyanins have weak phenol oxidase activity further supports the idea of close affinity [16, 17, 21, 22]. Just such a difference has been noted by comparing the crystal structure of sweet potato catechol oxidase with that of molluscan hemocyanin [15]
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