Characterization of the ubiquinone binding site in the alternative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling.

@article{Murai2010CharacterizationOT,
  title={Characterization of the ubiquinone binding site in the alternative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling.},
  author={Masatoshi Murai and Tetsuo Yamashita and Mai Senoh and Yuko Mashimo and Michihiko Kataoka and Hiroaki Kosaka and Akemi Matsuno-Yagi and Takao Yagi and Hideto Miyoshi},
  journal={Biochemistry},
  year={2010},
  volume={49 13},
  pages={
          2973-80
        }
}
The Ndi1 enzyme found in the mitochondrial membrane of Saccharomyces cerevisiae is an NDH-2-type alternative NADH-quinone oxidoreductase. As Ndi1 is expected to be a possible remedy for complex I defects of mammalian mitochondria, a detailed biochemical characterization of the enzyme is needed. To identify the ubiquinone (UQ) binding site in Ndi1, we conducted photoaffinity labeling using a photoreactive biotinylated UQ mimic (compound 2) synthesized following a concept of the least possible… CONTINUE READING

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