The Orange Carotenoid Protein: a blue-green light photoactive protein
The Orange Carotenoid Protein: a blue-green light photoactive protein
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DOI：
10.1039/c3pp25406b
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发表时间：
2013-01-01
影响因子：
3.1
通讯作者：
Kerfeld, Cheryl A.
中科院分区：
文献类型：
--
作者：
Kirilovsky, Diana;Kerfeld, Cheryl A.
本文综述了橙子类胡萝卜素蛋白（OCP），它是第一个被鉴定的含有类胡萝卜素作为光响应发色团的光活性蛋白。这种蛋白质是必不可少的触发蓝藻的光保护机制，减少了多余的吸收能量到达光合反应中心，通过增加热耗散的藻胆体，蓝藻天线的水平。蓝绿光引起类胡萝卜素和蛋白质的结构变化，将橙子非活性形式转化为红色活性形式。激活的红色形式与藻胆体相互作用，并诱导藻胆体荧光发射和到达光合反应中心的能量的减少。OCP是光传感器、信号传播器和能量猝灭器。第二种蛋白质，荧光恢复蛋白（FRP），需要将红色OCP从藻胆体中分离出来，并将其还原为无活性的橙子形式。在过去的十年中，结合结构和基因组数据的体内和体外机制研究导致了OCP和OCP介导的光保护功能的发现和详细描述。最近的结构和功能的结果强调和重要的以前的结果将进行审查。将讨论与其他蓝光响应蛋白的相似性。
This review focuses on the Orange Carotenoid Protein (OCP) which is the first photoactive protein identified containing a carotenoid as the photoresponsive chromophore. This protein is essential for the triggering of a photoprotective mechanism in cyanobacteria which decreases the excess absorbed energy arriving at the photosynthetic reaction centers by increasing thermal dissipation at the level of the phycobilisomes, the cyanobacterial antenna. Blue-green light causes structural changes within the carotenoid and the protein, converting the orange inactive form into a red active form. The activated red form interacts with the phycobilisome and induces the decrease of phycobilisome fluorescence emission and of the energy arriving to the photosynthetic reaction centers. The OCP is the light sensor, the signal propagator and the energy quencher. A second protein, the Fluorescence Recovery Protein (FRP), is needed to detach the red OCP from the phycobilisome and its reversion to the inactive orange form. In the last decade, in vivo and in vitro mechanistic studies combined with structural and genomic data resulted in both the discovery and a detailed picture of the function of the OCP and OCP-mediated photoprotection. Recent structural and functional results are emphasized and important previous results will be reviewed. Similarities to other blue-light responsive proteins will be discussed.