Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus
Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus
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长聚热聚球藻活性 NDH 复合物的酶学表征
DOI：
10.1016/j.febslet.2013.05.040
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发表时间：
2013-08-02
期刊：
影响因子：
3.5
通讯作者：
Mi Hualing
中科院分区：
文献类型：
--
作者：
Hu, Peng;Lv, Jing;Mi Hualing
虽然在植物和蓝藻中已经报道了1型NAD(P)H脱氢酶(NDH)复合亚单位的组成和生理功能，但该酶的生化性质尚不清楚。我们用层析分离的方法从长蓝藻中分离纯化并鉴定了一种具有NADPH活性的NDH。铁氧还蛋白(Fd)和铁氧还蛋白-NADP4(+)氧化还原酶(FNR)与NDH共洗脱，表明NADPH通过与FNR相互作用向NDH供电子。我们对该复合体的酶性质进行了研究。此外，该活性被鱼藤酮竞争性抑制，表明它具有一个醌结合位点，类似于线粒体复合体I(C)2013欧洲生化学会联合会。爱思唯尔出版，版权所有。
Although type-1 NAD(P)H dehydrogenase (NDH) complex subunit constituents and physiological functions have been reported in plants and cyanobacteria, the biochemical properties of this enzyme are not clear. We used chromatographic isolation to purify and characterize a NADPH-active NDH from the cyanobacterium Thermosynechococcus elongatus. Ferredoxin (Fd) and ferredoxin-NADP4(+) oxidoreductase (FNR) were co-eluted with NDH, implying the electron donation from NADPH to NDH via the interaction with FNR. We investigated the enzymatic properties of the complex. Furthermore, the activity is competitively inhibited by rotenone, suggesting that it possesses a quinone binding site, similar to mitochondria complex I. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.