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At least 217 records · Page 12Linked to original sources
PubMed1991

Degradation of organic sulfur compounds by a coal-solubilizing fungus.

Paecilomyces sp. TLi, a coal-solubilizing fungus, was shown to degrade organic sulfur-containing coal substructure compounds. Dibenzothiophene was degraded via a sulfur-oxidizing pathway to 2,2'-dihydroxybiphenyl. No further metabolism of that compound was observed. Ethyl phenyl sulfide and diphenyl sulfide were degraded to the corresponding sulfones. A variety of products were formed from dibenzyl sulfide, presumably via free radical intermediates. Diphenyl disulfide and dibenzyl disulfide were cleaved to the corresponding thiols and other single-ring products. It was concluded that degradation of organic sulfur compounds by Paecilomyces involves an oxidative attack localized at the sulfur atom.

Biodegradation, Environmental↗
PubMed2001

S K- and Mo L-edge X-ray absorption spectroscopy to determine metal-ligand charge distribution in molybdenum-sulfur compounds.

Mo L-edge and S K-edge X-ray absorption spectroscopy were applied to investigate the charge distribution between Mo and S in a series of Mo thiolate compounds, which serve as amide-sulfur H-bonding models and exhibit different redox potentials arising from polar group effects and ligand hydrogen bonds near the redox center. For all oxidized complexes, the S K-edge spectra exhibit a thiolate-based pre-edge feature centered at 2470.2 eV and the inflection point oCCurs at 2472.0 eV. No intense pre-edge feature is observed in the spectra for the reduced Mo model compounds and the energy shift of the S K-edge position depends on the S-ligand. Correlations between ligand charge density and the redox potential of the Mo-S cores are observed.

Ligands↗
PubMed1977

Effect of organic sulfur compounds on the chemical and enzymatic transformations of prostaglandin endoperoxide H2.

The effects of several sulfur organic compounds on the enzymatic and non-enzymatic transformations of prostaglandin endoperoxide H2 to prostaglandins were studied. Mercaptoethanol, methional alpha-lipoic acid and dimercaptopropanol increased the chemical (i.e. non-enzymatic) reduction of prostaglandin H2 to prostaglandin F2alpha but except for alpha-lipoic acid, had no effect on the enzymatic conversion of prostaglandin H2 to prostaglandin. In contrast, reduced glutathione showed no effect on the chemical conversion of prostaglandin H2, but exerted a marked and specific stimulation on the enzymatic isomerization of prostaglandin H2 to prostaglandin E2. This specific effect of gluthione may serve to regulate the overall intracellular activity of prostaglandin synthetase as well as the particular ratio of prostaglandins produced.

Animals↗