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本文引用的文献

1
Exploring the binding site of acetogenin in the ND1 subunit of bovine mitochondrial complex I.探索乙酸原在牛线粒体复合体I的ND1亚基中的结合位点。
Biochim Biophys Acta. 2009 Sep;1787(9):1106-11. doi: 10.1016/j.bbabio.2009.02.016. Epub 2009 Mar 2.
2
Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor.使用喹唑啉型抑制剂通过光亲和标记法对线粒体NADH-泛醌氧化还原酶中抑制剂结合位点的表征
Biochemistry. 2009 Feb 3;48(4):688-98. doi: 10.1021/bi8019977.
3
Binding is not enough: flexibility is needed for photocrosslinking of Lck kinase by benzophenone photoligands.仅结合是不够的：二苯甲酮光配体对Lck激酶进行光交联需要灵活性。
Bioorg Med Chem. 2008 Oct 1;16(19):8824-9. doi: 10.1016/j.bmc.2008.08.077. Epub 2008 Sep 3.
4
Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I.将线粒体ND3亚基鉴定为参与呼吸复合体I活性/非活性酶转变的结构成分。
J Biol Chem. 2008 Jul 25;283(30):20907-13. doi: 10.1074/jbc.M803190200. Epub 2008 May 23.
5
The ND1 subunit constructs the inhibitor binding domain in bovine heart mitochondrial complex I.ND1亚基构建了牛心脏线粒体复合体I中的抑制剂结合结构域。
Biochemistry. 2007 May 29;46(21):6409-16. doi: 10.1021/bi7003697. Epub 2007 May 3.
6
Blue native PAGE.蓝色非变性聚丙烯酰胺凝胶电泳
Nat Protoc. 2006;1(1):418-28. doi: 10.1038/nprot.2006.62.
7
Tricine-SDS-PAGE.三羟甲基氨基甲烷-十二烷基硫酸钠-聚丙烯酰胺凝胶电泳
Nat Protoc. 2006;1(1):16-22. doi: 10.1038/nprot.2006.4.
8
Analysis of the synaptic vesicle proteome using three gel-based protein separation techniques.使用三种基于凝胶的蛋白质分离技术对突触小泡蛋白质组进行分析。
Proteomics. 2006 Dec;6(23):6250-62. doi: 10.1002/pmic.200600357.
9
Bovine complex I is a complex of 45 different subunits.牛复合体I是一个由45种不同亚基组成的复合体。
J Biol Chem. 2006 Oct 27;281(43):32724-7. doi: 10.1074/jbc.M607135200. Epub 2006 Sep 1.
10
Energy converting NADH:quinone oxidoreductase (complex I).能量转换型NADH：醌氧化还原酶（复合体I）。
Annu Rev Biochem. 2006;75:69-92. doi: 10.1146/annurev.biochem.75.103004.142539.

ND2 亚基被鱼藤酮的一种光亲和类似物标记，鱼藤酮是一种有效的复合物 I 抑制剂。

The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor.

机构信息

Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.

出版信息

FEBS Lett. 2010 Mar 5;584(5):883-8. doi: 10.1016/j.febslet.2010.01.004. Epub 2010 Jan 13.

DOI:10.1016/j.febslet.2010.01.004
PMID:20074573
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2836797/
Abstract

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.

摘要

烟酰胺腺嘌呤二核苷酸

泛醌氧化还原酶（复合体 I）是线粒体氧化磷酸化的入口酶。为了获得抑制剂/醌结合位点的结构信息，我们合成了[3H]苯并酮-asi 霉素([3H]BPA)，这是 asi 霉素的光亲和类似物，asi 霉素属于被称为最有效的复合体 I 抑制剂的乙酰生酮家族。我们发现[3H]BPA 通过牛心亚线粒体颗粒的三维分离（蓝色非变性/双重 SDS-PAGE）与 ND2、ND1 和 ND5 亚基发生光交联。这种交联被鱼藤酮所阻断。这是首次发现 ND2 与一种强效的复合体 I 抑制剂发生光交联，表明它参与了抑制剂/醌结合。