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  • Title: Specificities of the two center N inhibitors of mitochondial bc1 complex, antimycin and funiculosin: strong involvement of cytochrome b-asparagine-208 in funiculosin binding.
    Author: Brasseur G, Brivet-Chevillotte P.
    Journal: FEBS Lett; 1994 Oct 31; 354(1):23-9. PubMed ID: 7957895.
    Abstract:
    Funiculosin, a center N inhibitor of the bc1 complex, induces a blue-shift in the cytochrome b spectrum. A thermosensitive revertant [Coppee, J.Y. et al., J. Biol. Chem. 269 (1994) 4221-4226] isolated from a cytochrome b respiratory-deficient mutant, exhibits a red-shift instead of the blue-shift retained in the original mutant and shows resistance to this inhibitor. Replacing cytochrome b-Asparagine-208 by Lysine in this revertant, keeping the original mutation S206L, leads, when mitochondria are incubated at non-permissive temperature, to complete loss of bc1 complex activity and funiculosin-binding, while the antimycin-binding is conserved. These data suggest some inhibitor site specificity and close proximity between the funiculosin-binding site and the catalytic center N domain (QN).
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