Biologically related iron-sulfur clusters as reaction centers. Reduction of acetylene to ethylene in systems based on [Fe4S4(SR)4]3-.

The possibility that clusters containing the Fe4S4 core unit found in a wide variety of proteins can effect reductive transformations of Fe-S enzyme substrates has been investigated using the reduced synthetic clusters [Fe4S4(SPh)4]3- and acetylene, an alternate nitrogenase substrate. The system [Fe4S4(SPh)4]3-/acetic acid/acetic anhydride in N-methylpyrollidinone at approximately 25 degrees was found to reduce acetylene homogeneously to ethylene, and in the presence of a deuterium source to afford as the principal stereochemical product cis-1,2-C2H2D2. No appreciable reduction was found using the oxidized cluster [Fe4S4(SPh)4]2-. The system is not catalytic and departs from the strict stoichiometry of the reaction, 2[Fe4S4(SPh)4]3- + C2H2 + 2H+ leads to 2 [Fe4S4(SPh)4]2- + C2H4, primarily because of a competing cluster oxidation reaction which could not be eliminated. Based on this reaction ca. 60% conversion of acetylene to ethylene was achieved. A reaction sequence based on absorption and 1H nmr spectral observations and product stereo-chemistry is suggested. The results demonstrate that biologically related, reduced Fe4S4 clusters can effect reduction of at least one Fe-S enzyme substrate, and raise the general possibility of substrate transformation with such clusters as reaction sites in biological systems.