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


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.

SUBMITTER: Nakamaru-Ogiso E 

PROVIDER: S-EPMC2836797 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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

Nakamaru-Ogiso Eiko E   Han Hongna H   Matsuno-Yagi Akemi A   Keinan Ehud E   Sinha Subhash C SC   Yagi Takao T   Ohnishi Tomoko T  

FEBS letters 20100113 5


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 [  ...[more]

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