Absorption spectra of photoactive yellow protein chromophores in vacuum
Absorption spectra of photoactive yellow protein chromophores in vacuum
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DOI：
10.1529/biophysj.105.061192
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发表时间：
2005-10-01
影响因子：
3.4
通讯作者：
Andersen, LH
中科院分区：
文献类型：
--
作者：
Nielsen, IB;Boyé-Péronne, S;Andersen, LH
用静电离子储存环在真空中测量了两个光活性黄色蛋白质模型发色团的吸收光谱。分离的发色团的吸收光谱是推断蛋白质环境对发色团电子能级的影响以及区分发色团的固有性质和蛋白质环境诱导的性质的重要参考。在真空中，去质子化的反硫苯基对香豆酸模型发色团在460 nm处有最大吸收，而光活性黄色蛋白在446 nm处有最大吸收。因此，蛋白质环境只会使吸收略有蓝移。相反，模型发色团在水溶液中的吸收显著蓝移(最大吸收波长395 nm)。还研究了去质子化的反式-对香豆酸，以阐明硫酯形成和苯酚去质子化的影响。在真空和水溶液中，发色团的这两个变化的总和都会引起红移。
The absorption spectra of two photoactive yellow protein model chromophores have been measured in vacuum using an electrostatic ion storage ring. The absorption spectrum of the isolated chromophore is an important reference for deducing the influence of the protein environment on the electronic energy levels of the chromophore and separating the intrinsic properties of the chromophore from properties induced by the protein environment. In vacuum the deprotonated transthiophenyl-p-coumarate model chromophore has an absorption maximum at 460 nm, whereas the photoactive yellow protein absorbs maximally at 446 nm. The protein environment thus only slightly blue-shifts the absorption. In contrast, the absorption of the model chromophore in aqueous solution is significantly blue-shifted (lambda(max) 395 nm). A deprotonated trans-p-coumaric acid has also been studied to elucidate the effect of thioester formation and phenol deprotonation. The sum of these two changes on the chromophore induces a red shift both in vacuum and in aqueous solution.