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- W4253090348 abstract "Enzymically active subcomplexes were purified from bovine mitochondrial NADH: ubiquinone oxidoreductase (complex I) by sucrose-gradient centrifugation in the presence of detergents. These subcomplexes, named Iλ, IS, and IλS, catalyse ferricyanide and ubiquinone-1 (Q-1) reduction by NADH at similar rates to complex I, but do not catalyse the reduction of decylubiquinone. In addition, the Q-1 reductase activity of all the subcomplexes is insensitive to rotenone. Chemical and EPR analyses of the subcomplexes show that FMN and all the Fe-S clusters of complex I are present, but that the line shape of cluster 2 is modified. The smallest subcomplex, IλS, contains only approximately 13 subunits, as compared to approximately 22 in the previously described sub-complex Iα [Finel, M., Skehel, J. M., Albracht, S. J. P., Fearnley, I. M. & Walker, J. E. (1992) Biochemistry 31, 11425–11434], but it retains the 75, 51-, 49-, 30-, 24-, 23- (TYKY) and 20-kDa (PSST) subunits, which are suggested to form a functional core that comprises the EPR-detectable Fe-S clusters 1–4, and FMN. The structural and functional implications of such an arrangement are discussed." @default.
- W4253090348 created "2022-05-12" @default.
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- W4253090348 date "2008-06-28" @default.
- W4253090348 modified "2023-09-25" @default.
- W4253090348 title "Isolation and Characterisation of Subcomplexes of the Mitochondrial NADH: Ubiquinone Oxidoreductase (Complex I)" @default.
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- W4253090348 doi "https://doi.org/10.1111/j.1432-1033.1994.0t237.x" @default.
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