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Default Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei

Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.

Related Articles Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.

FEBS Lett. 1995 Mar 27;362(1):34-8

Authors: Weesie RJ, Askin D, Jansen FJ, de Groot HJ, Lugtenburg J, Britton G

MAS (magic angle spinning) 13C NMR has been used to study protein-chromophore interactions in alpha-crustacyanin, the blue astaxanthin-binding carotenoprotein of the lobster, Homarus gammarus, reconstituted with astaxanthins labelled with 13C at the 14,14' or 15,15' positions. Two signals are seen for alpha-crustacyanin containing [14,14'-13C2]astaxanthin, shifted 6.9 and 4.0 ppm downfield from the 134.1 ppm signal of uncomplexed astaxanthin in the solid state. With alpha-crustacyanin containing [15,15'-13C2]astaxanthin, one essentially unshifted broad signal is seen. Hence binding to the protein causes a decrease in electronic charge density, providing the first experimental evidence that a charge redistribution mechanism contributes to the bathochromic shift of the astaxanthin in alpha-crustacyanin, in agreement with inferences based on resonance Raman data [Salares, et al. (1979) Biochim. Biophys. Acta 576, 176-191]. The splitting of the 14 and 14' signals provides evidence for asymmetric binding of each astaxanthin molecule by the protein.

PMID: 7698348 [PubMed - indexed for MEDLINE]



Source: PubMed
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