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• W2008032256 abstract "MAS (magic angle spinning) 13 C NMR has been used to study protein‐chromophore interactions in α‐crustacyanin, the blue astaxanthin‐binding carotenoprotein of the lobster, Homarus gammarus , reconstituted with astaxanthins labelled with 13 C at the 14,14′ or 15,15′ positions. Two signals are seen for α‐crustacyanin containing [14,14′‐ 13 C 2 ]astaxanthin, shifted 6.9 and 4.0 ppm downfield from the 134.1 ppm signal of uncomplexed astaxanthin in the solid state. With α‐crustacyanin containing [15,15′‐ 13 C 2 ]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 α‐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." @default.
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• W2008032256 date "1995-03-27" @default.
• W2008032256 modified "2023-10-15" @default.
• W2008032256 title "Protein-chromophore interactions in α-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, <i>Homarus gammarus</i> a study by ¹³ C magic angle spinning NMR" @default.
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• W2008032256 doi "https://doi.org/10.1016/0014-5793(95)00191-b" @default.
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