期刊
FEBS LETTERS
卷 584, 期 5, 页码 883-888出版社
WILEY
DOI: 10.1016/j.febslet.2010.01.004
关键词
Complex I; Bovine heart mitochondria; Asimicin; ND2; Photoaffinity labeling; Quinone binding
资金
- U.S. Public Health Service [R01GM33712, R01GM030736]
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 [H-3] benzophenone-asimicin ([H-3]BPA), a photoaffinity analogue of asimicin, which belongs to the acetogenin family known as the most potent complex I inhibitor. We found that [H-3] BPA was photo-crosslinked to ND2, ND1 and ND5 subunits, by the three dimensional separation (bluenative/doubled SDS-PAGE) of [H-3] BPA-treated bovine heart submitochondrial particles. The crosslinking 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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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