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The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor
Author(s) -
Nakamaru-Ogiso Eiko,
Han Hongna,
Matsuno-Yagi Akemi,
Keinan Ehud,
Sinha Subhash C.,
Yagi Takao,
Ohnishi Tomoko
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.01.004
Subject(s) - submitochondrial particle , photoaffinity labeling , chemistry , benzophenone , inhibitor protein , rotenone , protein subunit , oxidative phosphorylation , stereochemistry , anthraquinones , quinone , electron transport complex i , affinity label , oxidoreductase , nadh dehydrogenase , biochemistry , mitochondrion , enzyme , binding site , biology , photochemistry , botany , gene
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 [ 3 H]benzophenone‐asimicin ([ 3 H]BPA), a photoaffinity analogue of asimicin, which belongs to the acetogenin family known as the most potent complex I inhibitor. We found that [ 3 H]BPA was photo‐crosslinked to ND2, ND1 and ND5 subunits, by the three dimensional separation (blue‐native/doubled SDS–PAGE) of [ 3 H]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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