Redox signaling in chloroplasts:: Cleavage of disulfides by an iron-sulfur cluster
Redox signaling in chloroplasts:: Cleavage of disulfides by an iron-sulfur cluster
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DOI：
10.1126/science.287.5453.655
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发表时间：
2000-01-28
期刊：
影响因子：
56.9
通讯作者：
Eklund, H
中科院分区：
文献类型：
--
作者：
Dai, SD;Schwendtmayer, C;Eklund, H
光在叶绿体中产生还原当量，其不仅用于碳还原，而且用于通过铁氧还蛋白：硫氧还蛋白还原酶（FTR）系统还原调节性二硫化物来调节叶绿体酶的活性。FTR是该途径中的关键电子/巯基转换酶，其独特之处在于它可以通过铁-硫簇还原二硫化物，这一特性可以通过其活性位点二硫化物和铁-硫中心的紧密接触来解释。薄的扁平FTR分子通过在一侧与硫氧还蛋白形成混合二硫化物并通过在相对侧提供铁氧还蛋白的通路以递送电子而使双电子还原成为可能。
Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system, FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a property that is explained by the tight contact of its active-site disulfide and the iron-sulfur center. The thin, flat FTR molecule makes the two-electron reduction possible by forming on one side a mixed disulfide with thioredoxin and by providing on the opposite side access to ferredoxin for delivering electrons.