Suppr超能文献

亲水性光系统II组装蛋白Psb27、Psb28和Ycf48的结构与功能

Structure and function of the hydrophilic Photosystem II assembly proteins: Psb27, Psb28 and Ycf48.

作者信息

Mabbitt Peter D, Wilbanks Sigurd M, Eaton-Rye Julian J

机构信息

Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin, New Zealand.

Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin, New Zealand.

出版信息

Plant Physiol Biochem. 2014 Aug;81:96-107. doi: 10.1016/j.plaphy.2014.02.013. Epub 2014 Feb 25.

Abstract

Photosystem II (PS II) is a macromolecular complex responsible for light-driven oxidation of water and reduction of plastoquinone as part of the photosynthetic electron transport chain found in thylakoid membranes. Each PS II complex is composed of at least 20 protein subunits and over 80 cofactors. The biogenesis of PS II requires further hydrophilic and membrane-spanning proteins which are not part of the active holoenzyme. Many of these biogenesis proteins make transient interactions with specific PS II assembly intermediates: sometimes these are essential for biogenesis while in other examples they are required for optimizing assembly of the mature complex. In this review the function and structure of the Psb27, Psb28 and Ycf48 hydrophilic assembly factors is discussed by combining structural, biochemical and physiological information. Each of these assembly factors has homologues in all oxygenic photosynthetic organisms. We provide a simple overview for the roles of these protein factors in cyanobacterial PS II assembly emphasizing their participation in both photosystem biogenesis and recovery from photodamage.

摘要

光系统II(PS II)是一种大分子复合物,作为类囊体膜中光合电子传递链的一部分,负责光驱动的水氧化和质体醌还原。每个PS II复合物由至少20个蛋白质亚基和80多种辅因子组成。PS II的生物合成需要其他亲水性和跨膜蛋白,这些蛋白不是活性全酶的一部分。许多这些生物合成蛋白与特定的PS II组装中间体进行短暂相互作用:有时这些相互作用对生物合成至关重要,而在其他情况下,它们是优化成熟复合物组装所必需的。在本综述中,通过结合结构、生化和生理信息,讨论了Psb27、Psb28和Ycf48亲水性组装因子的功能和结构。这些组装因子在所有产氧光合生物中都有同源物。我们简要概述了这些蛋白质因子在蓝藻PS II组装中的作用,强调它们在光系统生物合成和光损伤恢复中的参与。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验