Dynamics of oxidation of inorganic sulphur compounds in upper soil horizons of spruce forests

1981 ◽  
Vol 26 (1) ◽  
pp. 24-28 ◽  
Author(s):  
A. Lettl ◽  
O. Langkramer ◽  
V. Lochman
2004 ◽  
Vol 2 (2) ◽  
pp. 278-289 ◽  
Author(s):  
Robert Pietrzak ◽  
Mieczysław Kozłowski ◽  
Helena Wachowska ◽  
Jan Yperman

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.


1985 ◽  
Vol 17 (1) ◽  
pp. 29-38 ◽  
Author(s):  
L J Webb

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.


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.


Nature ◽  
1987 ◽  
Vol 326 (6116) ◽  
pp. 891-892 ◽  
Author(s):  
Friedhelm Bak ◽  
Heribert Cypionka

1981 ◽  
Vol 26 (1) ◽  
pp. 29-36 ◽  
Author(s):  
A. Lettl ◽  
O. Langkramer ◽  
V. Lochman ◽  
M. Jakš

2002 ◽  
Vol 30 (4) ◽  
pp. 638-642 ◽  
Author(s):  
V. A. Bamford ◽  
B. C. Berks ◽  
A. M. Hemmings

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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