Electronic absorption, magnetic circular dichroism, and resonance Raman spectroscopies have been used to determine the nature of oxomolybdenum-thiolate bonding in (PPh4)[MoO(SPh)4] (SPh = phenylthiolate) and (HNEt3)[MoO(SPh-PhS)2] (SPh-PhS = biphenyl-2,2'-dithiolate). These compounds, like all oxomolybdenum tetraarylthiolate complexes previously reported, display an intense low-energy charge-transfer feature that we have now shown to be comprised of multiple S-->Mo dxy transitions. The integrated intensity of this low-energy band in [MoO(SPh)4]- is approximately twice that of [MoO(SPh-PhS)2]-, implying a greater covalent reduction of the effective nuclear charge localized on the molybdenum ion of the former and a concomitant negative shift in the Mo(V)/Mo(IV) reduction potential brought about by the differential S-->Mo dxy charge donation. However, this is not observed experimentally; the Mo(V)/Mo(IV) reduction potential of [MoO(SPh)4]- is approximately 120 mV more positive than that of [MoO(SPh-PhS)2]- (-783 vs -900 mV). Additional electronic factors as well as structural reorganizational factors appear to play a role in these reduction potential differences. Density functional theory calculations indicate that the electronic contribution results from a greater sigma-mediated charge donation to unfilled higher energy molybdenum acceptor orbitals, and this is reflected in the increased energies of the [MoO(SPh-PhS)2]- ligand-to-metal charge-transfer transitions relative to those of [MoO(SPh)4]-. The degree of S-Mo dxy covalency is a function of the O identical to Mo-S-C dihedral angle, with increasing charge donation to Mo dxy and increasing charge-transfer intensity occurring as the dihedral angle decreases from 90 to 0 degree. These results have implications regarding the role of the coordinated cysteine residue in sulfite oxidase. Although the O identical to Mo-S-C dihedral angles are either approximately 59 or approximately 121 degrees in these oxomolybdenum tetraarylthiolate complexes, the crystal structure of the enzyme reveals an O identical to Mo-SCys-C angle of approximately 90 degrees. Thus, a significant reduction in SCys-Mo dxy covalency is anticipated in sulfite oxidase. This is postulated to preclude the direct involvement of coordinated cysteine in coupling the active site into efficient superexchange pathways for electron transfer, provided the O identical to Mo-SCys-C angle is not dynamic during the course of catalysis. Therefore, we propose that a primary role for coordinated cysteine in sulfite oxidase is to statically poise the reduced molybdenum center at more negative reduction potentials in order to thermodynamically facilitate electron transfer from Mo(IV) to the endogenous b-type heme.

The electronic structure of a genuine paramagnetic des-oxo Mo(V) catalytic intermediate in the reaction of dimethyl sulfoxide reductase (DMSOR) with (CH3)3NO has been probed by EPR, electronic absorption and MCD spectroscopies. EPR spectroscopy reveals rhombic g- and A-tensors that indicate a low-symmetry geometry for this intermediate and a singly occupied molecular orbital (SOMO) that is dominantly metal centered. The excited state spectroscopic data were interpreted in the context of electronic structure calculations, and this has resulted in a full assignment of the observed magnetic circular dichroism (MCD) and electronic absorption bands, a detailed understanding of the metal-ligand bonding scheme, and an evaluation of the Mo(V) coordination geometry and Mo(V)-Sdithiolene covalency as it pertains to the stability of the intermediate and electron transfer regeneration. Finally, the relationship between des-oxo Mo(V) and des-oxo Mo(IV) geometric and electronic structures is discussed relative to the reaction coordinate in members of the DMSOR enzyme family.

Heme-Cu/O2 adducts are of interest in the elucidation of the fundamental metal-O2 chemistry occurring in heme-Cu enzymes which effect reductive O-O cleavage of dioxygen to water. In this report, the chemistry of four heme-peroxo-copper [FeIII-(O22-)-CuII]+ complexes (1-4), varying in their ligand architecture, copper-ligand denticity, or both and thus their structures and physical properties are compared in their reactivity toward CO, PPh3, acids, cobaltocene, and phenols. In 1 and 2, the copper(II) ligand is N4-tetradentate, and the peroxo unit is bound side-on to iron(III) and end-on to the copper(II). In contrast, 3 and 4 contain a N3-tridentate copper(II) ligand, and the peroxo unit is bound side-on to both metal ions. CO "displaces" the peroxo ligand from 2-4 to form reduced CO-FeII and CO-CuI species. PPh3 reacts with 3 and 4 displacing the peroxide ligand from copper, forming (porphyrinate)FeIII-superoxide plus CuI-PPh3 species. Complex 2 does not react with PPh3, and surprisingly, 1 reacts neither with PPh3 nor CO, exhibiting remarkable stability toward these reagents. The behavior of 1 and 2 compared to that of 3 and 4 correlates with the different denticity of the copper ligand (tetra vs tridentate). Complexes 1-4 react with HCl releasing H2O2, demonstrating the basic character of the peroxide ligand. Cobaltocene causes the two-electron reduction of 1-4 giving the corresponding micro-oxo [FeIII-(O2-)-CuII]+ complexes, in contrast to the findings for other heme-peroxo-copper species of different design. With t-butyl-substituted phenols, no reaction occurs with 1-4. The results described here emphasize how ligand design and variations influence and control not only the structure and physical properties but also the reactivity patterns for heme-Cu/O2 adducts. Implications for future investigations of protonated heme/Cu-peroxo complexes, low-spin analogues, and ultimately O-O cleavage chemistry are discussed.

X-ray crystallography and resonance Raman (rR) spectroscopy have been used to further characterize (Tp*)MoO(qdt) (Tp* is hydrotris(3,5-dimethyl-1-pyrazolyl)borate and qdt is 2,3-quinoxalinedithiolene), which represents an important benchmark oxomolybdenum mono-dithiolene model system relevant to various pyranopterin Mo enzyme active sites, including sulfite oxidase. The compound (Tp*)MoO(qdt) crystallizes in the triclinic space group, P1, where a = 9.8424 (7) A, b = 11.2323 (8) A, c = 11.9408 (8) A, alpha = 92.7560 (10) degrees, beta = 98.9530 (10) degrees, and gamma = 104.1680 (10) degrees. The (Tp*)MoO(qdt) molecule exhibits the distorted six-coordinate geometry characteristic of related oxo-Mo(V) systems possessing a single coordinated dithiolene ligand. The first coordination sphere bond lengths and angles in (Tp*)MoO(qdt) are very similar to the corresponding structural parameters for (Tp*)MoO(bdt) (bdt is 1,2-benzenedithiolene). The relatively small inner-sphere structural variations observed between (Tp*)MoO(qdt) and (Tp*)MoO(bdt) strongly suggest that geometric effects are not a major contributor to the significant electronic structural differences reported for these two oxo-Mo(V) dithiolenes. Therefore, the large differences observed in the reduction potential and first ionization energy between the two molecules appear to derive primarily from differences in the effective nuclear charges of their respective sulfur donors. However, a subtle perturbation to Mo-S bonding is implied by the nonplanarity of the dithiolene chelate ring, which is defined by the fold angle. This angular distortion (theta = 29.5 degrees in (Tp*)MoO(qdt); 21.3 degrees in (Tp*)MoO(bdt)) observed between the MoS2 and S-C=C-S planes may contribute to the electronic structure of these oxo-Mo dithiolene systems by controlling the extent of S p-Mo d orbital overlap. In enzymes, the fold angle may be dynamically modulated by the pyranopterin, thereby functioning as a transducer of vibrational energy associated with protein conformational changes directly to the active site via changes in the fold angle. This process could effectively mediate charge redistribution at the active site during the course of atom- and electron-transfer processes. The rR spectrum shows bands at 348 and 407 cm(-1). From frequency analysis of the normal modes of the model, [(NH3)3MoO(qdt)]1+, using the Gaussian03 suite of programs, these bands are assigned as mixed-mode Mo-S vibrations of the five-membered Mo-ditholene core structure. Raman spectroscopy has also provided additional evidence for an in-plane pseudo-sigma dithiolene S-Mo d(xy) covalent bonding interaction in (Tp*)MoO(qdt) and related oxo-Mo-dithiolenes that has implications for electron-transfer regeneration of the active site in sulfite oxidase involving the pyranopterin dithiolene.