Hypercoordinated organotin compounds containing sulfur and chlorine. Molcular structures of [(Ph3P)2N]+[S(SnR2Cl)2Cl]- (R=Me, t-Bu)

The reaction of diorganotin sulfides, cyclo-(R₂SnS)_n (R=Me, n-Bu; n=3; R=t-Bu; n=2) with the corresponding diorganotin dichlorides, R₂SnCl₂, provided the tetraorganodistannathianes, (R₂ClSn)₂S (1, R=Me; 2, R=n-Bu; 3, R=t-Bu). ¹H-, ¹³C-, and ¹¹⁹Sn-NMR studies indicate that these compounds are kinetically labile and in equilibrium with the starting materials. Addition of equimolar amounts of [(Ph₃P)₂N]Cl to the reaction mixtures gave the chloride complexes [(Ph₃P)₂N]⁺[S(SnR₂Cl)₂Cl]⁻ (4, R=Me; 5, R=n-Bu; 6, R=t-Bu). Single-crystal X-ray diffraction studies revealed the tin atoms in both 4 and 6 to adopt distorted trigonal bipyramidal configurations with the chlorine atoms occupying the axial positions.

End-Permian catastrophe by a bolide impact: evidence of a gigantic release of sulfur from the mantle

Our studies in southern China have revealed a remarkable sulfur and strontium isotope excursion at the end of the Permian, along with a coincident concentration of impact- metamorphosed grains and kaolinite and a significant decrease in manganese, phosphorous, calcium, and microfossils (foraminifera). These data suggest that an asteroid or a comet hit the ocean at the end of Permian time and caused a rapid and massive release of sulfur from the mantle to the ocean-atmosphere system, leading to significant oxygen consumption, acid rain, and the most severe biotic crisis in the history of life on Earth.

Sulfur and heavy metals in biological tissue

The correlation between sulfur, metallothionein and heavy metals was investigated in biological samples from the aquatic environment. Samples of orange roughie, shark, goldfish and king crab were analysed for metals and sulfur. Results indicated that there was insufficient evidence to suggest any relationship between sulfur and total metals, but there was sufficient evidence to suggest a significant relationship existed between mercury and total sulfur in the biological tissues examined.

Sulfur-doped porous reduced graphene oxide hollow nanosphere frameworks as metal-free electrocatalysts for oxygen reduction reaction and as supercapacitor electrode materials.

Chemical doping with foreign atoms is an effective approach to significantly enhance the electrochemical performance of the carbon materials. Herein, sulfur-doped three-dimensional (3D) porous reduced graphene oxide (RGO) hollow nanosphere frameworks (S-PGHS) are fabricated by directly annealing graphene oxide (GO)-encapsulated amino-modified SiO2 nanoparticles with dibenzyl disulfide (DBDS), followed by hydrofluoric acid etching. The XPS and Raman spectra confirmed that sulfur atoms were successfully introduced into the PGHS framework via covalent bonds. The as-prepared S-PGHS has been demonstrated to be an efficient metal-free electrocatalyst for oxygen reduction reaction (ORR) with the activity comparable to that of commercial Pt/C (40%) and much better methanol tolerance and durability, and to be a supercapacitor electrode material with a high specific capacitance of 343 F g(-1), good rate capability and excellent cycling stability in aqueous electrolytes. The impressive performance for ORR and supercapacitors is believed to be due to the synergistic effect caused by sulfur-doping enhancing the electrochemical activity and 3D porous hollow nanosphere framework structures facilitating ion diffusion and electronic transfer.

Sulfur-impregnated, sandwich-type, hybrid carbon nanosheets with hierarchical porous structure for high-performance lithium-sulfur batteries

Sandwich-type hybrid carbon nanosheets (SCNMM) consisting of graphene and micro/mesoporous carbon layer are fabricated via a double template method using graphene oxide as the shape-directing agent and SiO2 nanoparticles as the mesoporous guide. The polypyrrole synthesized in situ on the graphene oxide sheets is used as a carbon precursor. The micro/mesoporous strcutures of the SCNMM are created by a carbonization process followed by HF solution etching and KOH treatment. Sulfur is impregnated into the hybrid carbon nanosheets to generate S@SCNMM composites for the cathode materials in Li-S secondary batteries. The microstructures and electrochemical performance of the as-prepared samples are investigated in detail. The hybrid carbon nanosheets, which have a thickness of about 10-25 nm, high surface area of 1588 m2 g-1, and broad pore size distribution of 0.8-6.0 nm, are highly interconnected to form a 3D hierarchical structure. The S@SCNMM sample with the sulfur content of 74 wt% exhibits excellent electrochemical performance, including large reversible capacity, good cycling stability and coulombic efficiency, and good rate capability, which is believed to be due to the structure of hybrid carbon materials with hierarchical porous structure, which have large specific surface area and pore volume.

Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I)

Glutaredoxins have been characterised as enzymes regulating the redox status of protein thiols via cofactors GSSG/GSH. However, such a function has not been demonstrated with physiologically relevant protein substrates in in vitro experiments. Their active sites frequently feature a Cys-xx-Cys motif that is predicted not to bind metal ions. Such motifs are also present in copper-transporting proteins such as Atox1, a human cytosolic copper metallo-chaperone. In this work, we present the first demonstration that: (i) human glutaredoxin 1 (hGrx1) efficiently catalyses interchange of the dithiol and disulfide forms of the Cys(12)-xx-Cys(15) fragment in Atox1 but does not act upon the isolated single residue Cys(41); (ii) the direction of catalysis is regulated by the GSSG/2GSH ratio and the availability of Cu(I); (iii) the active site Cys(23)-xx-Cys(26) in hGrx1 can bind Cu(I) tightly with femtomolar affinity (K(D) = 10(-15.5) M) and possesses a reduction potential of E(o)' = -118 mV at pH 7.0. In contrast, the Cys(12)-xx-Cys(15) motif in Atox1 has a higher affinity for Cu(I) (K(D) = 10(-17.4) M) and a more negative potential (E(o)' = -188 mV). These differences may be attributed primarily to the very low pKa of Cys23 in hGrx1 and allow rationalisation of conclusion (ii) above: hGrx1 may catalyse the oxidation of Atox1(dithiol) by GSSG, but not the complementary reduction of the oxidised Atox1(disulfide) by GSH unless Cu(aq)(+) is present at a concentration that allows binding of Cu(I) to reduced Atox1 but not to hGrx1. In fact, in the latter case, the catalytic preferences are reversed. Both Cys residues in the active site of hGrx1 are essential for the high affinity Cu(I) binding but the single Cys(23) residue only is required for the redox catalytic function. The molecular properties of both Atox1 and hGrx1 are consistent with a correlation between copper homeostasis and redox sulfur chemistry, as suggested by recent cell experiments. These proteins appear to have evolved the features necessary to fill multiple roles in redox regulation, Cu(I) buffering and Cu(I) transport.