Department of Biological Sciences, Division of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, LA 70803, USA.
J Photochem Photobiol B. 2011 Jul-Aug;104(1-2):165-78. doi: 10.1016/j.jphotobiol.2011.01.025. Epub 2011 Feb 25.
Numerous studies over the last 25 years have established that the extrinsic PsbO, PsbP and PsbQ proteins of Photosystem II play critically important roles in maintaining optimal manganese, calcium and chloride concentrations at the active site of Photosystem II. Chemical or genetic removal of these components induces multiple and profound defects in Photosystem II function and oxygen-evolving complex stability. Recently, a number of studies have indicated possible additional roles for these proteins within the photosystem. These include putative enzymatic activities, regulation of reaction center protein turnover, modulation of thylakoid membrane architecture, the mediation of PS II assembly/stability, and effects on the reducing side of the photosystem. In this review we will critically examine the findings which support these auxiliary functions and suggest additional lines of investigations which could clarify the nature of the functional interactions of these proteins with the photosystem.
在过去的 25 年中，许多研究已经证实，光系统 II 的外在 PsbO、PsbP 和 PsbQ 蛋白在维持光系统 II 活性位点的最佳锰、钙和氯浓度方面起着至关重要的作用。这些组件的化学或遗传去除会导致光系统 II 功能和产氧复合物稳定性的多种和深刻缺陷。最近，一些研究表明这些蛋白质在光合作用系统中可能具有其他作用。这些作用包括假定的酶活性、反应中心蛋白周转率的调节、类囊体膜结构的调制、PS II 组装/稳定性的介导以及对光系统还原侧的影响。在这篇综述中，我们将批判性地检查支持这些辅助功能的发现，并提出其他的研究方向，以澄清这些蛋白质与光合作用系统相互作用的性质。
