Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR
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 fo...
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crwiley:10.1016/0014-5793(95)00191-b 2024-06-23T07:53:33+00:00 Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR Weesie, R.J Askin, D Jansen, F.J.H.M de Groot, H.J.M Lugtenburg, J Britton, G 1995 http://dx.doi.org/10.1016/0014-5793(95)00191-b https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2895%2900191-B https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(95)00191-B https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2895%2900191-B en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor FEBS Letters volume 362, issue 1, page 34-38 ISSN 0014-5793 1873-3468 journal-article 1995 crwiley https://doi.org/10.1016/0014-5793(95)00191-b 2024-06-13T04:22:31Z 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. Article in Journal/Newspaper Homarus gammarus Wiley Online Library FEBS Letters 362 1 34 38 |
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Wiley Online Library |
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English |
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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. |
format |
Article in Journal/Newspaper |
author |
Weesie, R.J Askin, D Jansen, F.J.H.M de Groot, H.J.M Lugtenburg, J Britton, G |
spellingShingle |
Weesie, R.J Askin, D Jansen, F.J.H.M de Groot, H.J.M Lugtenburg, J Britton, G Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR |
author_facet |
Weesie, R.J Askin, D Jansen, F.J.H.M de Groot, H.J.M Lugtenburg, J Britton, G |
author_sort |
Weesie, R.J |
title |
Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR |
title_short |
Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR |
title_full |
Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR |
title_fullStr |
Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR |
title_full_unstemmed |
Protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus a study by 13 C magic angle spinning NMR |
title_sort |
protein‐chromophore interactions in α‐crustacyanin, the major blue carotenoprotein from the carapace of the lobster, homarus gammarus a study by 13 c magic angle spinning nmr |
publisher |
Wiley |
publishDate |
1995 |
url |
http://dx.doi.org/10.1016/0014-5793(95)00191-b https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2895%2900191-B https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(95)00191-B https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2895%2900191-B |
genre |
Homarus gammarus |
genre_facet |
Homarus gammarus |
op_source |
FEBS Letters volume 362, issue 1, page 34-38 ISSN 0014-5793 1873-3468 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1016/0014-5793(95)00191-b |
container_title |
FEBS Letters |
container_volume |
362 |
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1 |
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34 |
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38 |
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1802645266679988224 |