Redox regulation in the chloroplast thylakoid lumen: a new frontier in photosynthesis research
Redox regulation in the chloroplast thylakoid lumen: a new frontier in photosynthesis research
复制标题
DOI：
10.1093/jxb/eri158
复制
发表时间：
2005-06-01
影响因子：
6.9
通讯作者：
Luan, S
中科院分区：
文献类型：
--
作者：
Buchanan, BB;Luan, S
最初与光合作用有关，现在已知通过改变硫醇基团（S-S 2SH）的氧化还原状态进行调节在整个生物学中都存在。因此，除了发挥重要的结构和催化功能外，人们还认识到，在许多情况下，二硫键可以被破坏和重组以进行调节。几个系统，每个将氢供体与中间二硫键蛋白质连接起来，通过改变硫醇氧化还原状态来实现改变目标蛋白质活性的变化。与当前讨论相关的是叶绿体铁氧还蛋白/硫氧还蛋白系统，由光还原铁氧还蛋白、硫氧还蛋白和存在于基质中的铁氧还蛋白-硫氧还蛋白还原酶组成。在该系统中，硫氧还蛋白将酶的活性与光联系起来：那些在生物合成中起作用的酶通过硫氧还蛋白被光还原激活（S-S -> 2SH），而在降解中起作用的酶在光照条件下失活并在黑暗中被氧化激活（2SH -> S-S）。最近的研究发现了一种新的范例，其中亲免素、FKBP13 和叶绿体类囊体腔的其他潜在酶在光下被氧化激活 (2SH -> S-S)。本综述提供了对这项近期工作的看法。
Initially linked to photosynthesis, regulation by change in the redox state of thiol groups (S-S 2SH) is now known to occur throughout biology. Thus, in addition to serving important structural and catalytic functions, it is recognized that, in many cases, disulphide bonds can be broken and reformed for regulation. Several systems, each linking a hydrogen donor to an intermediary disulphide protein, act to effect changes that alter the activity of target proteins by change in the thiol redox state. Pertinent to the present discussion is the chloroplast ferredoxin/thioredoxin system, comprised of photoreduced ferredoxin, a thioredoxin, and the enzyme ferredoxin-thioredoxin reductase, that occur in the stroma. In this system, thioredoxin links the activity of enzymes to light: those enzymes functional in biosynthesis are reductively activated by light via thioredoxin (S-S -> 2SH), whereas counterparts acting in degradation are deactivated under illumination conditions and are oxidatively activated in the dark (2SH -> S-S). Recent research has uncovered a new paradigm in which an immunophilin, FKBP13, and potentially other enzymes of the chloroplast thylakoid lumen are oxidatively activated in the light (2SH -> S-S). The present review provides a perspective on this recent work.