Spectroscopic and electronic structure studies of symmetrized models for reduced members of the dimethylsulfoxide reductase enzyme family.

Enzymes belonging to the dimethylsulfoxide reductase (DMSOR) family of pyranopterin Mo enzymes have a unique active-site geometry in the reduced form that lacks a terminal oxo ligand, unlike the reduced active sites of other pyranopterin Mo enzymes. Furthermore, the DMSOR family is characterized by the coordination of two pyranopterin-ene-1,2-dithiolate ligands in their active sites, which is distinctive among the other pyranopterin Mo enzymes but analogous to all of the currently known tungsten-containing enzymes. Electronic absorption, resonance Raman, and ground- and excited-state density functional calculations of symmetrized analogues of the reduced DMSOR active site ([NEt4][Mo(IV)(QAd)(S2C2Me2)2] where Ad = 2-adamantyl; Q = O, S, Se) have allowed for a detailed description of Mo-bisdithiolene electronic structure in the absence of a strong-field oxo ligand. The electronic absorption spectra are dominated by dithiolene S --> Mo charge-transfer transitions, and the totally symmetric Mo-S Raman stretch is observed at approximately 400 cm(-1) for all three complexes. These data indicate that the Mo-bisdithiolene bonding scheme in high-symmetry [Mo(QAd)(S2C2Me2)2]- complexes is not strongly perturbed by the apical QAd- ligands, but instead, the dithiolene ligands define the t(2g) ligand field splitting. The effects of conserved geometric distortions observed in DMSOR, relative to these high-symmetry models, were explored by spectroscopically calibrated bonding calculations, and the results are discussed within the context of electronic structure contributions to ground-state destabilization and transition-state stabilization. The specific electronic structure tuning of the endogenous amino acid ligation on the mechanism of DMSOR is also discussed.

Synthesis and characterization of volatile, thermally stable, reactive transition metal amidinates.

A series of homoleptic metal amidinates of the general type [M(R-R'AMD)(n)](x) (R = (i)Pr, (t)Bu, R' = Me, (t)Bu) has been prepared and structurally characterized for the transition metals Ti, V, Mn, Fe, Co, Ni, Cu, Ag, and La. In oxidation state 3, monomeric structures were found for the metals Ti(III), V(III), and La(III). Bridging structures were observed for the metals in oxidation state 1. Cu(I) and Ag(I) are held in bridged dimers, and Ag(I) also formed a trimer that cocrystallized with the dimer. Metals in oxidation state 2 occurred in either monomeric or dimeric form. Metals with smaller ionic radii (Co, Ni) were monomeric. Larger metals (Fe, Mn) gave monomeric structures only with the bulkier tert-butyl-substituted amidinates, while the less bulky isopropyl-substituted amidinates formed dimers. The new compounds were found to have properties well-suited for use as precursors for atomic layer deposition (ALD) of thin films. They have high volatility, high thermal stability, and high and properly self-limited reactivity with molecular hydrogen, depositing pure metals, or water vapor, depositing metal oxides.

Atomic layer deposition of transition metals.

Atomic layer deposition (ALD) is a process for depositing highly uniform and conformal thin films by alternating exposures of a surface to vapours of two chemical reactants. ALD processes have been successfully demonstrated for many metal compounds, but for only very few pure metals. Here we demonstrate processes for the ALD of transition metals including copper, cobalt, iron and nickel. Homoleptic N,N'-dialkylacetamidinato metal compounds and molecular hydrogen gas were used as the reactants. Their surface reactions were found to be complementary and self-limiting, thus providing highly uniform thicknesses and conformal coating of long, narrow holes. We propose that these ALD layers grow by a hydrogenation mechanism that should also operate during the ALD of many other metals. The use of water vapour in place of hydrogen gas gives highly uniform, conformal films of metal oxides, including lanthanum oxide. These processes should permit the improved production of many devices for which the ALD process has previously not been applicable.

X-ray absorption spectroscopy of a structural analogue of the oxidized active sites in the sulfite oxidase enzyme family and related molybdenum(V) complexes.

X-ray absorption spectroscopy (XAS) (edge and extended X-ray absorption fine structure (EXAFS)) has been applied to the characterization of three molybdenum(V,VI) monodithiolene complexes with unidentate coligands, [MoO(SC(6)H(2)-2,4,6-Pr(i)()(3))(2)(bdt)](-) (1), [MoOCl(SC(6)H(2)-2,4,6-Pr(i)(3))(bdt)](-) (2), and [MoO(2)(SC(6)H(2)-2,4,6-Pr(i)(3))(bdt)](-) (3) (bdt = benzene-1,2-dithiolate). These complexes are related to the active site in the xanthine oxidase and sulfite oxidase families and, as in the enzyme sites, bind monodentate thiolate. By comparison to the data of crystalline oxidized chicken sulfite oxidase, it is shown that complex 3, whose thiolate simulates binding by the highly conserved cysteine, is an accurate structural analogue of the oxidized site of this enzyme. Normalized edge spectra, EXAFS data, Fourier transforms, and GNXAS-based fit results are presented. As in earlier studies, this provides characterization of new analogue complexes by XAS to facilitate identification of related sites in proteins.

Description of the ground state wave functions of Ni dithiolenes using sulfur K-edge X-ray absorption spectroscopy.

The pterin-dithiolene cofactor is an essential component of the catalytic sites of all molybdoenzymes except nitrogenase. Understanding its bonding to transition metals allows for development of electronic structure/function correlations in catalysis. The electronic structure description for a series of bis(dithiolene) complexes ([NiL(2)](Z)(), L = 1,2-Me(2)C(2)S(2); Z = 2-, 1-, 0) using sulfur XAS provides the basis for extension to the biologically relevant metal-containing dithiolenes. The transition dipole integral has been developed for the dithiolene sulfur through correlation of XAS pre-edge energy positions of sulfide-, thiolate-, and enedithiolate-S. The ground state wave functions of all three NiL(2) complexes have more than 50% S character experimentally demonstrating the noninnocent behavior of the dithiolene ligand. The S K-edge experimental results are correlated with spin-unrestricted, broken-symmetry density functional calculations. These show only limited spin polarization in the neutral complex and delocalized, ligand based ground states for the mono- and dianionic complexes. These XAS and DFT results are correlated with other spectroscopic features and provide insight into reactivity.

Molecular Heme-Cyanide-Copper Bridged Assemblies: Linkage Isomerism, Trends in nu(CN) Values, and Relation to the Heme-a(3)/Cu(B) Site in Cyanide-Inhibited Heme-Copper Oxidases.

Bovine heart cytochrome c oxidase and related heme copper oxidases are inhibited by cyanide, which binds at the binuclear heme-a(3)/Cu(B) site where dioxygen is reduced to water. To determine the mode of cyanide binding, heme-based binuclear complexes containing iron-cyanide-copper bridges in different oxidation states have been prepared by the reaction of [(py)(OEP)Fe(CN)] with Cu(II,I) precursors and structurally characterized by X-ray methods. Structures of two precursor complexes and two binuclear Cu(I)-CN-Cu(I) species are reported. The assembly [(py)(OEP)Fe-CN-Cu(Npy(3))](2+) has a nearly linear Fe(III)-CN-Cu(II) bridge containing low-spin Fe(III). The assemblies [(OEP)Fe-NC-Cu(MeNpy(2))](+) and [(OEP-CH(2)CN)Fe-NC-Cu(Npy(3))](+) exhibit the high-spin bridges Fe(III)-NC-Cu(I) and Fe(II)-NC-Cu(I), respectively. These are the first title bridges in these oxidation states. Bridge atom sequences are obtained from structural refinements of both linkage isomers; those for the reduced bridges are consistent with the soft-acid nature of Cu(I). Cyanide stretching frequencies respond to metal oxidation state and bridge geometry and, using data for solution and solid states, fall into the following ranges: Fe(III)-CN-Cu(II), 2120-2184 cm(-)(1) (11 examples); Fe(III)-NC-Cu(I), 2072-2100 cm(-)(1) (2 examples); Fe(II)-NC-Cu(I), 2099-2107 cm(-)(1) (1 example). These data are compared with nu(CN) values for the enzymes in different oxidation states. A nonlinear Fe(III)-CN-Cu(II) bridge (Cu-N-C = 150-160 degrees ) is consistent with the 2146-2152 cm(-)(1) range found for the fully oxidized enzymes. Bands that can be assigned with some certainty as Fe-CN vibrations in partially and fully reduced enzymes do not appear to correspond to Fe(III)-NC-Cu(I) and Fe(II)-NC-Cu(I) bridges but rather to Fe(II)-CN modes. The current work complements and extends our previous investigation (Scott and Holm, J. Am. Chem. Soc. 1994, 116, 11357) of linear and nonlinear Fe(III)-CN-Cu(II) bridges and is part of an investigation directed at providing a molecular basis of cyanide toxicity. (MeNpy(2) = bis(2-(2-pyridylethyl))methylamine; Npy(3) = tris(2-pyridylmethyl)amine; OEP = octaethylporphyrinate(2-), OEP-CH(2)CN = N-(cyanomethyl)octaethylporphyrinate(1-).)