Tryptophan fluorescence monitors structural changes accompanying signalling state formation in the photocycle of photoactive yellow protein
Tryptophan fluorescence monitors structural changes accompanying signalling state formation in the photocycle of photoactive yellow protein
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DOI：
10.1039/b401600a
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发表时间：
2004-01-01
影响因子：
3.1
通讯作者：
Hellingwerf, KJ
中科院分区：
文献类型：
--
作者：
Gensch, T;Hendriks, J;Hellingwerf, KJ
光活性黄色蛋白是盐生盐藻的一种小分子水溶性蓝光感受器蛋白，具有两个疏水核心的结构，其中主要的一个核心容纳其光敏发色团(p-香豆酸)，中间由一个β-折叠隔开。这种光感受器蛋白含有一个色氨酸残基(W119)，它位于中心β-折叠和其N-末端帽之间的界面上。W119在暗态Pg(lambda(Max)=328 nm；Phi(Fl)=0.01；几乎与pH无关)的荧光性质是典型的埋藏在疏水环境中的色氨酸的荧光性质，附近的氨基酸残基显著猝灭。信号态的形成导致pH依赖的荧光变化：在pH值
Photoactive yellow protein, a small, water-soluble blue-light absorbing photoreceptor protein from Ectothiorhodospira (Halorhodospira) halophila has a structure with two hydrophobic cores, of which the main one houses its light-sensitive chromophore (p-coumaric acid), separated by a central beta-sheet. This photoreceptor protein contains a single tryptophan residue (W119) that is situated at the interface between the central beta-sheet and its N-terminal cap. The fluorescence properties of W119 in the dark state pG (lambda(max)=328 nm; Phi(fl)=0.01; nearly pH-independent) are typical for a buried tryptophan in a hydrophobic environment with significant quenching by nearby amino acid residues. Signalling state formation leads to pH-dependent fluorescence changes: At pH values