Ontology highlight
ABSTRACT:
SUBMITTER: Nakamaru-Ogiso E
PROVIDER: S-EPMC2836797 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
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]