Spectroscopy and Quantum Chemical Modeling Reveal a Predominant Contribution of Excitonic Interactions to the Bathochromic Shift in α-Crustacyanin, the Blue Carotenoprotein in the Carapace of the Lobster Homarus gammarus.
To resolve the molecular basis of the coloration mechanism of α-crustacyanin, we used C- labeled astaxanthins as chromophores for solid-state C NMR and resonance Raman spectroscopy of [6,6',7,7']-C α-crustacyanin and [8,8',9,9',10,10',11,11',20,20']-C α-crustacyanin. We complement the experimental d...
| Publicado en: | Journal of the American Chemical Society Vol. 127; no. 5; pp. 1438 - 1446 |
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| Autores principales: | , , , , , , |
| Formato: | Artículo |
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American Chemical Society
2/9/2005
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| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=16097929&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 16097929 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 2/9/2005 vid: 127 iid: 5 pid: 997 pub: American Chemical Society artinfo: ui: 16097929 10.1021/ja045049+ ppf: 1438 ppct: 8 formats: tig: atl: Spectroscopy and Quantum Chemical Modeling Reveal a Predominant Contribution of Excitonic Interactions to the Bathochromic Shift in α-Crustacyanin, the Blue Carotenoprotein in the Carapace of the Lobster Homarus gammarus. aug: au: van Wijk, Arjan A. C. Spaans, Arnold Uzunbajakava, Natallia Otto, Cees De Groot, Huub J. M. Lugtenburg, Johan Buda, Francesco affil: Leiden University. University of Twente. Philips Research Laboratories, 5656 AA Eindhoven, The Netherlands. su: Homarus gammarus Spectrum analysis Raman spectroscopy Density functionals Electron distribution Proteins sug: subj: Homarus gammarus Spectrum analysis Raman spectroscopy Density functionals Electron distribution Proteins ab: To resolve the molecular basis of the coloration mechanism of α-crustacyanin, we used C- labeled astaxanthins as chromophores for solid-state C NMR and resonance Raman spectroscopy of [6,6',7,7']-C α-crustacyanin and [8,8',9,9',10,10',11,11',20,20']-C α-crustacyanin. We complement the experimental data with time-dependent density functional theory calculations on several models based on the structural information available for β-crustacyanin. The data rule out major changes and strong polarization effects in the ground-state electron density of astaxanthin upon binding to the protein. Conformational changes in the chromophore and hydrogen-bond interactions between the astaxanthin and the protein can account only for about one-third of the total bathochromic shift in α-crustacyanin. The exciton coupling due to the proximity of two astaxanthin chromophores is found to be large, suggesting that aggregation effects in the protein represent the primary source of the color change. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2005 holdings: @attributes: islocal: N |
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