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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >beta-Crustacyanin, the blue-purple carotenoprotein of lobster carapace: consideration of the bathochromic shift of the protein-bound astaxanthin.
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beta-Crustacyanin, the blue-purple carotenoprotein of lobster carapace: consideration of the bathochromic shift of the protein-bound astaxanthin.

机译：蓝紫色carotenoprotein beta-Crustacyanin龙虾甲壳:考虑蛋白结合的红移

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摘要

The crystal structure of a beta-crustacyanin allows an analysis of the various proposals for the mechanism of the bathochromic shift from orange to purple-blue of astaxanthin in this lobster carotenoprotein. Structural and previous chemical and biophysical studies suggest that extension of conjugation by coplanarization of the beta-ionone rings with the polyene chain and polarization resulting from hydrogen bonding at the C(4) and C(4') keto groups may be mainly responsible for the bathochromic shift. Additional contributions may arise from medium effects and possibly from bowing of the polyene chain on binding. Previous biophysical data revealing a somewhat symmetrical polarization of astaxanthin in crustacyanin are thereby also accounted for. A puzzling feature remains unexplained: the bathochromic shifts, larger than that of astaxanthin, shown by some cyclopentenedione carotenoids in reconstituted carotenoproteins. This mini review enlarges on the original analysis and conclusions of Cianci et al. [(2002), Proc. Natl Acad. Sci. USA, 99, 9795-9800].
机译：beta-crustacyanin的晶体结构允许一个分析的各种建议红移的机理橙色是深的虾青素龙虾carotenoprotein。化学和生物物理的研究表明扩展coplanarization接合的与多烯链和beta-ionone响了极化产生的氢键C(4)和C(4)酮组可能是主要负责红移。额外的贡献可能来自于媒体效果和可能从多烯的鞠躬链上的绑定。揭示一种对称的极化虾青素在crustacyanin从而也占了。解释:增色的转变,比虾青素,显示一些在重组cyclopentenedione类胡萝卜素carotenoproteins。Cianci最初的分析和结论议事et al . (2002), Natl Acad Sci。9795-9800].

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