Abstract.
The structural characteristics of oxy- and deoxy-hemocyanins have been investigated using X-ray absorption spectroscopy both in the near-edge (XANES) and for the first shell contribution in the EXAFS region. Several arthropodan and molluscan hemocyanins have been studied in order to trace the inter- and intra-phyla differences. The XANES spectra of oxy-hemocyanins of the different species are remarkably similar, consistent with a very strongly conserved co-ordination geometry of the copper active site. In contrast, small but significant differences are observed between the deoxy-forms of arthropodan and molluscan proteins. In particular, the XANES spectra of deoxy-arthropodan hemocyanins (with the exception of L. polyphemus Hc) show a more intense edge feature at approximately 8983 eV. This difference is tentatively assigned to a more planar geometry of the copper-ligands system in the arthropodan rather than in the molluscan proteins.
The first shell analysis of the EXAFS modulation is consistent with the presence of n=3Nε 2 imidazole nitrogens at an average distance of 1.92±0.03 Å from copper in all the deoxy-hemocyanins investigated.
Binding of dioxygen results for all hemocyanins in the increase of the number of first shell back-scattering atoms to n=5 with average distances of 1.93 Å. Alternatively, by separating the contribution of Nε 2 imidazole nitrogens and of peroxide O-atoms, n=3 ligands at 1.98±0.03 Å and n=2 ligands at 1.87±0.03 Å are found.
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Sabatucci, A., Ascone, I., Bubacco, L. et al. Comparison of the X-ray absorption properties of the binuclear active site of molluscan and arthropodan hemocyanins. J Biol Inorg Chem 7, 120–128 (2002). https://doi.org/10.1007/s007750100272
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DOI: https://doi.org/10.1007/s007750100272