A novel method for determining the chelation ability of the cysteine-containing peptides with 3,4-toluenedithiol. Application to [2Fe-2S]-ferredoxin model systems.

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The chelating ability of a bidentate ligand, Cys–X–Y–Cys (X, Y=amino acid residue), in 2Fe–2S peptide model complexes was examined by a ligand-exchange method using 3,4-toluenedithiol (tdt-H2) or o-xylene-α,α′-dithiol. The addition of tdt-H2 to an N,N-dimethylformamide solution of [Fe2S2(Z–cys–Ala–Ala–cys–OMe)2]2− results in the cleavage pf Fe–S* (S*=inorganic sulfur) bond and in the formation of hydrogen sulfide and mononuclear Fe(III) peptide thiolate complex, [Fe(Z–cys–Ala–Ala–cys–OMe)(tdt)]1−. In the case of [Fe2S2(Z–Ala–cys–OMe)4]2−, [Fe2S2(tdt)2]2− was obtained by the substitution of Z–Ala–Cys–OMe with the chelating reagent. On the other hand, o-xylene-α,α′-dithiol expels both Z–Cys–Ala–Ala–Cys–OMe and Z–Ala–Cys–OMe ligands from these complexes.
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