AI Article Synopsis
- NADH:ubiquinone oxidoreductase (complex I) is crucial for mitochondrial energy production and an important target for studying drug interactions.
- Researchers created a radioactive version of asimicin, a potent inhibitor of complex I, to investigate how it binds to mitochondrial components.
- They discovered that this inhibitor can bind to specific subunits of complex I (ND1, ND2, and ND5), with ND2 showing a significant interaction, marking it as a key player in binding processes.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836797 | PMC |
| http://dx.doi.org/10.1016/j.febslet.2010.01.004 | DOI Listing |
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