The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor.
The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor.
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DOI：
10.1016/j.febslet.2010.01.004
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发表时间：
2010-03-05
期刊：
影响因子：
3.5
通讯作者：
Ohnishi T
中科院分区：
文献类型：
--
作者：
Nakamaru-Ogiso E;Han H;Matsuno-Yagi A;Keinan E;Sinha SC;Yagi T;Ohnishi T
NADH：泛醌氧化还原酶（复合物I）是线粒体氧化磷酸化的进入酶。为了获得抑制剂/醌结合位点的结构信息，我们合成了[3 H]二苯甲酮-阿西米星（[3 H]BPA），阿西米星的光亲和类似物，其属于被称为最有效的复合物I抑制剂的丙酮家族。通过对[~ 3 H] BPA处理的牛心脏亚线粒体颗粒进行三维分离（蓝色-天然/双重SDS-PAGE），发现[~ 3 H]BPA与ND_2、ND_1和ND_5亚基发生了光交联。交联被鱼藤酮阻断。这是第一次发现ND 2与有效的复合物I抑制剂光交联，表明其参与抑制剂/醌结合。
NADH:ubiquinone oxidoreductase (complex I) is the entry enzyme of mitochondrial oxidative phosphorylation. To obtain the structural information on inhibitor/quinone binding sites, we synthesized [3H]benzophenone-asimicin ([3H]BPA), a photoaffinity analogue of asimicin, which belongs to the acetogenin family known as the most potent complex I inhibitor. We found that [3H]BPA was photo-crosslinked to ND2, ND1 and ND5 subunits, by the three dimensional separation (blue-native/doubled SDS-PAGE) of [3H]BPA-treated bovine heart submitochondrial particles. The cross-linking was blocked by rotenone. This is the first finding that ND2 was photo-crosslinked with a potent complex I inhibitor, suggesting its involvement in the inhibitor/quinone-binding.
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