High-nuclearity Mo-Fe-S clusters are of interest as potential synthetic precursors to the MoFe7S9 cofactor cluster of nitrogenase. In this context, the synthesis and properties of previously reported but sparsely described trinuclear [(edt)(2)M2FeS6](3-) (M = Mo (2), W (3)) and hexanuclear [(edt)(2)Mo2Fe4S9](4-) (4, edt = ethane-1,2-dithiolate; Zhang, Z.; et al. Kexue Tongbao 1987, 32, 1405) have been reexamined and extended. More accurate structures of 2-4 that confirm earlier findings have been determined. Detailed preparations (not previously available) are given for 2 and 3, whose structures exhibit the C-2 arrangement {[(edt)M(S)(mu(2)-S)(2)](2)Fe-III}(3-) with square pyramidal Mo(V) and tetrahedral Fe(III). Oxidation states follow fro M Fe-57 Mossbauer parameters and an S = (3)/(2) ground state from the EPR spectrum. The assembly system 2/3FeCl(3)/3Li(2)S/nNaSEt in methanol/acetonitrile (n = 4) affords (R4N)(4)[4] (R = Et, Bu; 70-80%). The structure of 4 contains the [Mo2Fe4(mu(2)-S)(6)(mu(3)-S)(2)(mu(4)-S)](0) core, with the same bridging pattern as the [Fe6S9](2-) core of [Fe6S9(SR)(2)](4-) (1), in overall C-2v symmetry. Cluster 4 supports a reversible three-member electron transfer series 4-/3-/2- with E-1/2 = -0.76 and -0.30 V in Me2SO. Oxidation of (Et4N)(4)[4] in DMF with 1 equiv of tropylium ion gives [(edt)(2)Mo(2)Fe(4)Sg](3-) (5) isolated as (Et4N)(3)[5].2DMF (75%). Alternatively, the assembly system (n = 3) gives the oxidized cluster directly as (Bu4N)(3)[5] (53%). Treatment of 5 with 1 equiv of [CP2Fe](1+) in DMF did not result in one-electron oxidation but instead produced heptanuclear [(edt)(2)Mo2Fe5S11](3-) (6), isolated as the Bu(4)N(+)salt (38%). Cluster 6 features the previously unknown core Mo2Fe5(mu(2)-S)(7)(mu(3)-S)(4) in molecular C2 symmetry. In 4-6, the (edt)MoS3 sites are distorted trigonal bipramidal and the FeS4 sites are distorted tetrahedral with all sulfide ligands bridging. Mossbauer spectroscopic data for 2 and 4-6 are reported; (mean) iron oxidation states increase in the order 4 < 5 approximate to 1 < 6 approximate to 2. Redox and spectroscopic data attributed earlier to clusters 2 and 4 are largely in disagreement with those determined in this work. The only iron and molybdenum-iron clusters with the same sulfide content as the iron-molybdenum cofactor of nitrogenase are [Fe6S9(SR)(2)](4-) and [(edt)(2)Mo2Fe4S9](3-4-).