光系统I的PSI-E亚基结合铁氧化还原蛋白：NADP⁺氧化还原酶。
The PSI-E subunit of photosystem I binds ferredoxin:NADP+ oxidoreductase.
作者信息
Andersen B, Scheller H V, Møller B L
机构信息
Department of Plant Biology, Royal Veterinary and Agricultural University, Copenhagen, Denmark.
出版信息
FEBS Lett. 1992 Oct 19;311(2):169-73. doi: 10.1016/0014-5793(92)81391-x.
A photosystem I complex containing the polypeptides PSI-A to PSI-L, light-harvesting complex I and ferredoxin:NADP+ oxidoreductase has been isolated from barley using the non-ionic detergent n-decyl-beta-D-maltopyranoside. The ratio between bound ferredoxin:NADP+ oxidoreductase and P700 is 0.4 +/- 0.2. The complex is highly active in catalyzing light-induced transfer of electrons from plastocyanin to NADP+ at rates of 280 +/- 150 and 1800 +/- 800 mumol NADPH/(mg chl.h), without and in the presence of saturating amounts of exogenously added ferredoxin:NADP+ oxidoreductase, respectively. Endogenously bound ferredoxin:NADP+ oxidoreductase interacts with the PSI-E subunit as demonstrated by cross-linking experiments using two different types of cross-linkers and identification of the products by Western blotting and the use of monospecific antibodies.
使用非离子去污剂正癸基-β-D-麦芽糖苷从大麦中分离出了一种光系统I复合物，该复合物包含多肽PSI-A至PSI-L、光捕获复合物I和铁氧化还原蛋白：NADP⁺氧化还原酶。结合的铁氧化还原蛋白：NADP⁺氧化还原酶与P700的比例为0.4±0.2。该复合物在催化光诱导的电子从质体蓝素转移到NADP⁺方面具有很高的活性，在没有和存在饱和量的外源添加铁氧化还原蛋白：NADP⁺氧化还原酶的情况下，速率分别为280±150和1800±800 μmol NADPH/（mg叶绿素·小时）。通过使用两种不同类型的交联剂进行交联实验，并通过蛋白质印迹法和使用单特异性抗体鉴定产物，证明内源性结合的铁氧化还原蛋白：NADP⁺氧化还原酶与PSI-E亚基相互作用。
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