Thiosulfate oxidation by sulfur-grown Thiobacillus thiooxidans cells, cell-free extracts, and thiosulfate-oxidizing enzyme

1994 ◽  
Vol 40 (10) ◽  
pp. 816-822 ◽  
Author(s):  
C. W. Chan ◽  
Isamu Suzuki

The oxidation of thiosulfate by Thiobacillus thiooxidans grown on sulfur was studied in cells, cell-free extracts, and a thiosulfate-oxidizing enzyme system. Thiosulfate was oxidized to tetrathionate by cells treated with N-ethylmaleimide with a pH optimum at 2.3. The cell-free extracts also oxidized thiosulfate with the same pH optimum and O2 consumption. Untreated cells, on the other hand, oxidized thiosulfate to sulfite in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide, an inhibitor of sulfite oxidation. The cells treated with N-ethylmaleimide showed two Km values for thiosulfate while the cell-free system showed only one Km. The Km value for thiosulfate generally increased with the increasing pH. A soluble thiosulfate-oxidizing enzyme system was extracted from the cells at pH 2.5 in the presence of 1 M ammonium sulfate by passage through a French pressure cell. The system contained a native cytochrome c that was reduced by thiosulfate at pH 2.5 and a thiosulfate-ferricyanide oxidoreductase activity with a pH optimum around 2.0. The acidic extract also contained a component that reduced horse heart cytochrome c at a neutral pH. The reduction at an acidic pH required sulfite.Key words: thiosulfate oxidation, Thiobacillus thiooxidans, tetrathionate, sulfite.

1991 ◽  
Vol 56 (2) ◽  
pp. 478-490 ◽  
Author(s):  
Joaquin F. Perez-Benito ◽  
Conchita Arias

The reaction between horse-heart cytochrome c and ascorbic acid has been investigated in the pH range 5.5 – 7.1 and at 10.0 – 25.0 °C. The rate shows a first-order dependence on the concentration of cytochrome c, it increases in a non-linear way as the concentration of ascorbic acid increases, it increases markedly with increasing pH and, provided that the ionic strength of the medium is high enough, it fulfills the Arrhenius equation. The apparent activation energy increases as the pH of the solution increases. The results have been explained by means of a mechanism that includes the existence of an equilibrium between two forms (acidic and basic) of oxidized cytochrome c: cyt-H+ -Fe3+ + OH- cyt -Fe3+ + H2O, whose equilibrium constant is (6.7 ± 1.4). 108 at 25.0 °C, the acidic form being more reducible than the basic one. It is suggested that there is a linkage of hydrogenascorbate ion to both forms of cytochrome c previous to the redox reactions. Two possibilities for the oxidant-reductant linkage (binding and adsorption) are discussed in detail.


ChemInform ◽  
2010 ◽  
Vol 23 (27) ◽  
pp. no-no
Author(s):  
C. DI BELLO ◽  
C. VITA ◽  
L. GOZZINI

1994 ◽  
Vol 1 (6) ◽  
pp. 378-382 ◽  
Author(s):  
Phoebe Xiurong Qi ◽  
Jeffrey L. Urbauer ◽  
Ernesto J. Fuentes ◽  
Mary Frances Leopold ◽  
A. Joshua Wand

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