Abstract
A photoaffinity-labelling analogue of the respiratory inhibitor rotenone was synthesized from the naturally occurring rotenoid amorphigenin. The analogue inhibits NADH-ubiquinone oxidoreductase activity at concentrations comparable with those of rotenone. Photolysis of the radiolabelled analogue bound to isolated NADH-ubiquinone oxidoreductase resulted in preferential incorporation of radioactivity into a polypeptide of Mr 33 000, particularly at low concentrations of the inhibitor. Preparations of the enzyme differ in a parallel fashion in the content of this polypeptide, the degree of photolabelling by the analogue and their sensitivity to rotenone, providing further evidence that the 33 000-Mr protein forms part of the rotenone-binding site.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 4:46 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 25, 2021, 9:51 a.m.) |
Indexed | 2 months ago (June 27, 2025, 6:37 a.m.) |
Issued | 40 years, 8 months ago (Dec. 1, 1984) |
Published | 40 years, 8 months ago (Dec. 1, 1984) |
Published Print | 40 years, 8 months ago (Dec. 1, 1984) |
@article{Earley_1984, title={Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone}, volume={224}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2240525}, DOI={10.1042/bj2240525}, number={2}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Earley, F G P and Ragan, C I}, year={1984}, month=dec, pages={525–534} }