Conformational switching in a light-harvesting protein as followed by single-molecule spectroscopy.
Conformational switching in a light-harvesting protein as followed by single-molecule spectroscopy.
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DOI：
10.1016/j.bpj.2015.04.017
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发表时间：
2015-06-02
影响因子：
3.4
通讯作者：
van Grondelle, Rienk
中科院分区：
文献类型：
--
作者：
Gall, Andrew;Ilioaia, Cristian;Kruger, Tjaart P. J.;Novoderezhkin, Vladimir I.;Robert, Bruno;van Grondelle, Rienk
在蛋白质物理学的最终目标中，对导致蛋白质构象变化的能量路径进行完整的实验描述仍然是一个挑战。单蛋白荧光光谱构成了解决蛋白质动力学的一种选择方法，并且在天然荧光蛋白中，来自紫色细菌的捕光（LH）蛋白构成了这种研究的理想对象。LH结合细菌叶绿素a分子，这赋予它们高的固有荧光产率。此外，这些色素蛋白质的电子性质的结果，从他们的结合细菌叶绿素a分子之间的强激子耦合与大的能量紊乱，由于在其结构中的缓慢波动。因此，其荧光跃迁的位置和概率微妙地依赖于一组结合色素的无序的精确实现，这是由LH蛋白动力学控制的。使用时间分辨单分子荧光光谱分析这些参数，从而产生直接访问的蛋白质动力学。将该技术应用于Rhodovulum（Rdv.）sulfidophilum的结构和荧光性质取决于pH，使我们能够跟踪单一蛋白质，pH诱导的，可逆的，构象转变。因此，第一次，据我们所知，蛋白质转变可以通过内在辅因子的电子结构的变化来可视化，在单个LH蛋白质的水平上，这为我们了解能量景观的变化开辟了一条新的途径，这是蛋白质功能和适应生物体需求的基础。
Among the ultimate goals of protein physics, the complete, experimental description of the energy paths leading to protein conformational changes remains a challenge. Single protein fluorescence spectroscopy constitutes an approach of choice for addressing protein dynamics, and, among naturally fluorescing proteins, light-harvesting (LH) proteins from purple bacteria constitute an ideal object for such a study. LHs bind bacteriochlorophyll a molecules, which confer on them a high intrinsic fluorescence yield. Moreover, the electronic properties of these pigment-proteins result from the strong excitonic coupling between their bound bacteriochlorophyll a molecules in combination with the large energetic disorder due to slow fluctuations in their structure. As a result, the position and probability of their fluorescence transition delicately depends on the precise realization of the disorder of the set of bound pigments, which is governed by the LH protein dynamics. Analysis of these parameters using time-resolved single-molecule fluorescence spectroscopy thus yields direct access to the protein dynamics. Applying this technique to the LH2 protein from Rhodovulum (Rdv.) sulfidophilum, the structure—and consequently the fluorescence properties—of which depends on pH, allowed us to follow a single protein, pH-induced, reversible, conformational transition. Hence, for the first time, to our knowledge, a protein transition can be visualized through changes in the electronic structure of the intrinsic cofactors, at a level of a single LH protein, which opens a new, to our knowledge, route for understanding the changes in energy landscape that underlie protein function and adaptation to the needs of living organisms.
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DOI：
10.1016/0005-2728(90)90008-r
发表时间：
1990-03-15
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
EVANS, MB;HAWTHORNTHWAITE, AM;COGDELL, RJ
通讯作者：
COGDELL, RJ
影响因子：
3.7
作者：
Gall, A;Henry, S;Cogdell, RJ
通讯作者：
Cogdell, RJ
DOI：
10.1073/pnas.96.20.11271
发表时间：
1999-09-28
影响因子：
11.1
作者：
Bopp, MA;Sytnik, A;Hochstrasser, RM
通讯作者：
Hochstrasser, RM
影响因子：
3.4
作者：
Richter, Martin F.;Baier, Juergen;Oellerich, Silke
通讯作者：
Oellerich, Silke
影响因子：
3.3
作者：
Sauer, K;Cogdell, RJ;Scheer, H
通讯作者：
Scheer, H