Metabolism of inorganic sulphur compounds byThiobacillus ferrooxidans and some comparative studies onThiobacillus A2 andT. neapolitanus

1975 ◽  
Vol 43 (1-3) ◽  
pp. 77-93 ◽  
Author(s):  
D. P. Kelly ◽  
O. H. Tuovinen
Keyword(s):  
Comparative Studies ◽  
Sulphur Compounds ◽  
Inorganic Sulphur

scholarly journals Studies of the soluble part of oxidised coals

2004 ◽  
Vol 2 (2) ◽  
pp. 278-289 ◽  
Author(s):  
Robert Pietrzak ◽  
Mieczysław Kozłowski ◽  
Helena Wachowska ◽  
Jan Yperman
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Nitric Acid ◽  
Atmospheric Pressure ◽  
Temperature Programmed Reduction ◽  
Sulphur Compounds ◽  
Inorganic Sulphur ◽  
Temperature Programmed ◽  
Sulphur Species ◽  
Soluble Part

AbstractSoluble products obtained from the oxidation of four types of coal, each characterised by different degree of coalification and different degree of sulphur content, are studied. The coals are oxidised with peracetic acid (PAA) and nitric acid. Analyses are performed by Atmospheric Pressure-Temperature Programmed Reduction (AP-TPR) and Fourier Transform Infrared Spectroscopy (FTIR). The soluble products contain much more sulphur than the insoluble products of oxidation. The products obtained from the reaction with HNO3 contain higher amounts of inorganic sulphur compounds, while those obtained from the reaction with PAA are characterised by an increased content of organic sulphur species.

Characteristics of Paper/Board Mill Wastewaters Relevant to Anaerobic Treatment

1985 ◽  
Vol 17 (1) ◽  
pp. 29-38 ◽  
Author(s):  
L J Webb
Keyword(s):  
Suspended Solids ◽  
Anaerobic Fermentation ◽  
Analytical Data ◽  
Water System ◽  
Anaerobic Treatment ◽  
Sulphur Compounds ◽  
Toxic Materials ◽  
Dissolved Organics ◽  
Sizing System ◽  
Inorganic Sulphur

Apart from the inherent amenability of the organics present to anaerobic fermentation, a number of other factors are important to the technical and economic viability of the overall process. These include wastewater strength, wastewater temperature, the nature of suspended solids present and the presence of toxic materials, notably sulphates/sulphides and biocides. Analytical data is presented from various Pira research projects, describing the composition of UK mill wastewaters in terms of BOD/COD/DOC, suspended solids, the speciation of dissolved organics (eg carbohydrates, fatty acids) and inorganic sulphur compounds. In the context of anaerobic treatment, this is then discussed in terms of in-mill microbiological activity, the extent of water system closure and the type of sizing system employed.

Anaerobic oxidation of sulphur compounds as electron donors for bacterial photosynthesis

1982 ◽  
Vol 298 (1093) ◽  
pp. 529-542 ◽  
Keyword(s):  
Bacterial Photosynthesis ◽  
Elemental Sulphur ◽  
Electron Donors ◽  
Oxidative Enzymes ◽  
Sulphur Compounds ◽  
Anoxygenic Photosynthesis ◽  
Aps Reductase ◽  
Inorganic Sulphur ◽  
Sulphite Reductase ◽  
Haem Iron

Most phototrophic bacteria use reduced inorganic sulphur compounds as electron donors during anoxygenic photosynthesis. Principally, sulphide is oxidized via sulphite to sulphate. Elemental sulphur may appear as intermediary storage product (inside: Chromatium, Thiocapsa ; outside: Chlorbium, Ectothiorhodospira ; not in : Rhodopseudomonas sulfidophila ). Adenosine phosphosulphate is an intermediate in sulphite oxidation by Chromatium, Thiocapsa and Chlorobium . Thiosulphate undergoes splitting to sulphide (or elemental sulphur) and sulphite, or is oxidized to tetrathionate. Sulphide may be oxidized to elemental sulphur by cytochrome c or to thiosulphate (perhaps sulphite?) by flavocytochrome c , or to sulphite by a reverse (sirohaem) sulphite reductase. The latter enzyme also oxidizes polysulphides and probably elemental sulphur. Sulphite is either oxidized by APS reductase to form adenosine phosphosulphate - from which sulphate is released by ADP sulphurylase - or by sulphite: acceptor oxidoreductase directly to sulphate. The electron acceptor of most of these oxidative enzymes are cytochromes or non-haem iron-sulphur proteins. The pathways of photolithotrophic sulphur oxidation in Chlorobiaceae, Chromatiaceae and Rhodospirillaceae are separately compiled under evaluation of the presently available data.

A novel type of energy metabolism involving fermentation of inorganic sulphur compounds

Nature ◽  
1987 ◽  
Vol 326 (6116) ◽  
pp. 891-892 ◽  
Author(s):  
Friedhelm Bak ◽  
Heribert Cypionka
Keyword(s):  
Energy Metabolism ◽  
Sulphur Compounds ◽  
Inorganic Sulphur

Thiobacilli and sulphate production from inorganic sulphur compounds in upper horizons of spruce forest soils

1981 ◽  
Vol 26 (1) ◽  
pp. 29-36 ◽  
Author(s):  
A. Lettl ◽  
O. Langkramer ◽  
V. Lochman ◽  
M. Jakš
Keyword(s):  
Forest Soils ◽  
Spruce Forest ◽  
Sulphur Compounds ◽  
Inorganic Sulphur

Novel domain packing in the crystal structure of a thiosulphate-oxidizing enzyme

2002 ◽  
Vol 30 (4) ◽  
pp. 638-642 ◽  
Author(s):  
V. A. Bamford ◽  
B. C. Berks ◽  
A. M. Hemmings
Keyword(s):  
Crystal Structure ◽  
Photosynthetic Bacterium ◽  
Electron Donors ◽  
Sulphur Compounds ◽  
Rhodovulum Sulfidophilum ◽  
Sulphur Cycle ◽  
Electron Transport Chains ◽  
Inorganic Sulphur ◽  
Electron Transfer Complex ◽  
Respiratory Electron Transport

A key component of the oxidative biogeochemical sulphur cycle involves the utilization by bacteria of reduced inorganic sulphur compounds as electron donors to photosynthetic or respiratory electron transport chains. The SoxAX protein of the photosynthetic bacterium Rhodovulum sulfidophilum is a heterodimeric c-type cytochrome that is involved in the oxidation of thiosulphate and sulphide. The recently solved crystal structure of the SoxAX complex represents the first structurally characterized example of a productive electron transfer complex between haemoproteins where both partners adopt the c-type cytochrome fold. The packing of c-type cytochrome domains both within SoxA and at the interface between the subunits of the complex has been compared with other examples and found to be unique.

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