Active NDH-1 complexes from the cyanobacterium Synechocystis sp. strain PCC 6803.
Active NDH-1 complexes from the cyanobacterium Synechocystis sp. strain PCC 6803.
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DOI：
10.1093/pcp/pcl008
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发表时间：
2006-10
影响因子：
4.9
通讯作者：
Weimin Ma;Yong Deng;T. Ogawa;H. Mi
中科院分区：
文献类型：
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作者：
Weimin Ma;Yong Deng;T. Ogawa;H. Mi
我们确定了八个带染色天然凝胶的NADPH-硝基蓝四唑氧化还原酶活性电泳后，正十二烷基-β-d-麦芽糖苷处理的膜集胞藻属菌株PCC 6803。其中A、C、D、E四条酶带为NADPH脱氢酶（NDH-1）的酶带。条带A是NDH-1的高活性超复合物（约1，000 kDa），在DeltandhD 1/D2突变体中不存在，在低CO下受到抑制（2）。C带在低CO（2）条件下或DeltandhD 1/D2突变体中诱导，并转化为D带和E带。带A和C似乎分别是NDH-1 L二聚体和NDH-1 M，具有活性所必需的亚基。
We identified eight bands by staining native gels for NADPH-nitroblue tetrazolium oxidoreductase activity after electrophoresis of n-dodecyl-beta-d-maltoside-treated membranes of Synechocystis sp. strain PCC 6803. Among them, bands A, C, D and E were attributed to the activity of NADPH dehydrogenase (NDH-1). Band A is a highly active supercomplex of NDH-1 (about 1,000 kDa) that was absent in the DeltandhD1/D2 mutant and was suppressed under low CO(2). Band C was induced under low CO(2) or in the DeltandhD1/D2 mutant and was converted to bands D and E. Bands A and C appear to be an NDH-1L dimer and NDH-1M, respectively, with subunits essential for the activity.