Edward I. Stiefel

Bio: Edward I. Stiefel is an academic researcher from ExxonMobil. The author has contributed to research in topics: Molybdenum & Catalysis. The author has an hindex of 45, co-authored 170 publications receiving 5406 citations. Previous affiliations of Edward I. Stiefel include Kettering University.

Molybdenum sulfur antiwear and antioxidant lube additives

Abstract: In accordance with this invention, there is provided a lubricating composition comprising a major amount of an oil of lubricating viscosity and a minor amount of an additive having the formula Mo 2 L 4 wherein L is a ligand selected from xanthates and mixtures thereof and, in particular, xanthates having a sufficient number of carbon atoms to render the additive soluble in the oil. In general, the xanthate ligand, L, will have form about 2 to 30 carbon atoms.

A method for reducing viscosity increase in sooted diesel oils

Abstract: The present invention is directed to a method for improving the performance of a sooted diesel oil and controlling soot induced viscosity increase by adding to a major amount of a diesel oil a minor amount of a composition comprising at least one compound having the formula Mo3SkLnQz and mixtures thereof wherein the L are independently selected ligands having organo groups with a sufficient number of carbon atoms to render the compound soluble or dispersible in the oil, n is from 1 to 4, k varies from 4 through 10, Q is selected from the group of neutral electron donating compounds such as water, amines, alcohols, phosphines, and ethers, and z ranges from 0 to 5 and includes nonstoichiometric values.

Induced internal electron transfer reactivity of tetrathioperrhenate(VII): synthesis of the interconvertible dimers Re2(.mu.-S)2(S2CNR2)4 and [Re2(.mu.-SS2CNR2)2(S2CNR2)3][O3SCF3] (R = Me, iso-Bu)

Abstract: Rhenium sulfides, e.g., ReS{sub 2} and Re{sub 2}S{sub 7}, have long been recognized for their hydrogenation and dehydrogenation reactivity. Periodic trends in catalytic hydrodesulfurization (HDS) reveal rhenium sulfur systems to have high activity. However, discrete, soluble rhenium sulfur species have not received as much attention as have group VI sulfide systems. The tetrathiometalate anions of V, Mo, and W (VS{sub 4}{sup 3{minus}}; MoS{sub 4}{sup 2{minus}}; WS{sub 4}{sup 2{minus}}), which possess fully oxidized (d{sup 0}) metal centers and fully reduced (S{sup 2{minus}}) sulfide ligands, undergo internal redox upon reacting with external oxidants. In these reactions bound sulfide ions (S{sup 2{minus}}) serve as the reductant forming disulfide (S{sub 2}{sup 2{minus}}) concomitant with reduction of the metal center. Conspicuously, ReS{sub 4}{sup {minus}} is the only soluble tetrathiometalate whose chemistry in this regard has not been explored. Here the authors report that tetraalkylthiuram disulfide, acting as an oxidant, induces a dramatic and unprecedented 3e{sup {minus}} reduction of the Re-(VII) center of ReS{sub 4}{sup {minus}}.

[Cr4S(O2CCH3)8(H2O)4](BF4)2·H2O: Ferromagnetically Coupled Cr4S Cluster with Spin 6 Ground State

Abstract: Data on the preparation, structure, and magnetism of the new complex [Cr4S(O2CCH3)8(H2O)4](BF4)2⋅H2O are presented. The metal-sulfur M4S core structure is similar to that found in M4S[S2As(CH3)2]6 ...

Secondary building units, nets and bonding in the chemistry of metal–organic frameworks

Abstract: This critical review presents a comprehensive study of transition-metal carboxylate clusters which may serve as secondary building units (SBUs) towards construction and synthesis of metal–organic frameworks (MOFs). We describe the geometries of 131 SBUs, their connectivity and composition. This contribution presents a comprehensive list of the wide variety of transition-metal carboxylate clusters which may serve as secondary building units (SBUs) in the construction and synthesis of metal–organic frameworks. The SBUs discussed here were obtained from a search of molecules and extended structures archived in the Cambridge Structure Database (CSD, version 5.28, January 2007) which included only crystals containing metal carboxylate linkages (241 references).

The Mononuclear Molybdenum Enzymes

Abstract: Molybdenum is the only second-row transition metal required by most living organisms, and is nearly universally distributed in biology. Enzymes containing molybdenum in their active sites have long been recognized,1 and at present over 50 molybdenum-containing enzymes have been purified and biochemically characterized; a great many more gene products have been annotated as putative molybdenum-containing proteins on the basis of genomic and bioinformatic analysis.2 In certain cases, our understanding of the relationship between enzyme structure and function is such that we can speak with confidence as to the detailed nature of the reaction mechanism and, with the availability of high-resolution X-ray crystal structures, the specific means by which transition states are stabilized and reaction rate is accelerated within the friendly confines of the active site. At the same time, our understanding of the biosynthesis of the organic cofactor that accompanies molybdenum (variously called molybdopterin or pyranopterin), the manner in which molybdenum is incorporated into it, and then further modified as necessary prior to insertion into apoprotein has also (in at least some cases) become increasingly well understood. It is now well-established that all molybdenum-containing enzymes other than nitrogenase (in which molybdenum is incorporated into a [MoFe7S9] cluster of the active site) fall into three large and mutually exclusive families, as exemplified by the enzymes xanthine oxidase, sulfite oxidase, and DMSO reductase; these enzymes represent the focus of the present account.3 The structures of the three canonical molybdenum centers in their oxidized Mo(VI) states are shown in Figure 1, along with that for the pyranopterin cofactor. The active sites of members of the xanthine oxidase family have an LMoVIOS-(OH) structure with a square-pyramidal coordination geometry. The apical ligand is a Mo=O ligand, and the equatorial plane has two sulfurs from the enedithiolate side chain of the pyranopterin cofactor, a catalytically labile Mo–OH group, and most frequently a Mo=S. Nonfunctional forms of these enzymes exist in which the equatorial Mo=S is replaced with a second Mo=O; in at least one member of the family the Mo=S is replaced by a Mo=Se, and in others it is replaced by a more complex –S–Cu–S–Cys to give a binuclear center. Members of the sulfite oxidase family have a related LMoVIO2(S–Cys) active site, again square-pyramidal with an apical Mo=O and a bidentate enedithiolate Ligand (L) in the equatorial plane but with a second equatorial Mo=O (rather than Mo–OH) and a cysteine ligand contributed by the protein (rather than a Mo=S) completing the molybdenum coordination sphere. The final family is the most diverse structurally, although all members possess two (rather than just one) equiv of the pyranopterin cofactor and have an L2MoVIY(X) trigonal prismatic coordination geometry. DMSO reductase itself has a catalytically labile Mo=O as Y and a serinate ligand as X completing the metal coordination sphere of oxidized enzyme. Other family members have cysteine (the bacterial Nap periplasmic nitrate reductases), selenocysteine (formate dehydrogenase H), –OH (arsenite oxidase), or aspartate (the NarGHI dissimilatory nitrate reductases) in place of the serine. Some enzymes have S or even Se in place of the Mo=O group. Members of the DMSO reductase family exhibit a general structural homology to members of the aldehyde:ferredoxin oxidoreductase family of tungsten-containing enzymes;4 indeed, the first pyranopterin-containing enzyme to be crystallographically characterized was the tungsten-containing aldehyde:ferredoxin oxidoreductase from Pyrococcus furiosus,5 a fact accounting for why many workers in the field prefer “pyranopterin” (or, perhaps waggishly, “tungstopterin”) to “molybdopterin”. The term pyranopterin will generally be used in the present account. Open in a separate window Figure 1 Active site structures for the three families of mononuclear molybdenum enzymes. The structures shown are, from left to right, for xanthine oxidase, sulfite oxidase, and DMSO reductase. The structure of the pyranopterin cofactor common to all of these enzymes (as well as the tungsten-containing enzymes) is given at the bottom.