Results 161 to 170 of about 7,369 (206)

The Sulfite Oxidase of Thiobacillus ferrooxidans (Ferrobacillus ferrooxidans)

Canadian Journal of Biochemistry, 1971
The sulfite oxidase (sulfite: cytochrome c oxidoreductase) from sulfur-grown Thiobacillus ferrooxidans was isolated and partially purified, and its properties were studied. The enzyme was purified 7.3-fold and was 75–85% of the protein present. Sulfite oxidase required SO32− for activity, and could use horse heart cytochrome c and ferricyanide as ...
J R, Vestal, D G, Lundgren
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The rhodanese enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

Canadian Journal of Biochemistry, 1969
Extract of sulfur-grown Ferrobacillus ferrooxidans contains the thiosulfate-splitting enzyme rhodanese. Rhodanese was purified about 40-fold and was shown to have a wide pH optimum (pH 7.5–9.0). The Km for thiosulfate and cyanide was 5.8 × 10−4 M and 1.1 × 10−2 M, respectively.
R, Tabita, M, Silver, D G, Lundgren
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Reduction of dichromate by Thiobacillus ferrooxidans

Biotechnology Letters, 1996
Chromium(VI) was reduced by Thiobacillus ferrooxidans grown with elemental sulphur as the sole energy source. Chromium(VI) reduction (as high as 2000 μM), was due to the presence of sulphite and thiosulphate, among others with high reducing power which was generated during the sulphur oxidation by the bacteria.
F. Sisti, P. Allegretti, E. Donati
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Uranium resistance of Thiobacillus ferrooxidans

European Journal of Applied Microbiology and Biotechnology, 1983
The toxicity of uranium to several isolates of Thiobacillus ferrooxidans was determined. Plasmid DNA of approx. 13±0.5 megadaltons was detected in four cultures that exhibited the highest resistance to UO2 2+. One isolate, TFI-7, always contained a 13 megadalton plasmid and was always resistant to uranium.
Phyllis A. W. Martin, Patrick R. Dugan, Olli H. Tuovinen   +2 more
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Biosorption of Cu by Thiobacillus ferrooxidans

Bioprocess Engineering, 1998
Current technologies for removal and recovery of both toxic and industrial interest metals usually produce wastes with high concentrations of those substances. They are an important source of environmental pollution, specially when they contain heavy metals.
A. Ruiz-Manríquez, P. I. Magaña, V. López, R. Guzmán   +3 more
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[Thiobacillus ferrooxidans pili].

Mikrobiologiia, 1978
The surface structures of Thiobacillus ferrooxidans were studied. When growing on a medium containing elemental sulphur, the cells possess peritrichously located filaments (piles) whose diameter varies from 4.5 to 7.0 nm and length, from 0.7 to 3.0 mcm. The cells of T. ferrooxidans do not have piles on a medium with ferrous iron. The physiological role
L A, Gromova, N A, Pereverzev, G I, Karavaĭko   +2 more
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Combined degradation of covellite by Thiobacillus thiooxidans and Thiobacillus ferrooxidans

Biotechnology Letters, 1996
In the presence of iron, which is always associated with natural sulphide ores, the percentages of copper dissolution in the bioleaching of covellite were 34 and 45 % when Thiobacillus thiooxidans and Thiobacillus ferrooxidans were used together and when an indirect bioleaching with attached bacteria was performed respectively.
G. Curutchet, P. Tedesco, E. Donati
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Desulfurization of Coal by Thiobacillus Ferrooxidans

1980
Literature on the possibility of desulfurizing coal by microbiological leaching is limited. The earliest report was that of Zarubina et al. (1959) who indicated that 23 to 27% of sulfur was removed from their coal samples in 30 days. Other investigators (Silverman et al.
T. M. Olsen, P. R. Ashman, A. E. Torma, L. E. Murr   +3 more
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Sulfur-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

Canadian Journal of Biochemistry, 1968
The sulfur-oxidizing enzyme was purified about 15-fold from sulfur-grown Ferrobacillus ferrooxidans. The enzyme has a pH optimum of 7.8 and requires both elemental sulfur and reduced glutathione (GSH); however, a glutathione–polysulfide complex could also serve as substrate. The Km for GSH was determined to be 2 × 10−3 M.
M, Silver, D G, Lundgren
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The soluble adenosine triphosphatase of Thiobacillus ferrooxidans

Canadian Journal of Microbiology, 1975
Adenosine triphosphatase (ATPase) from Thiobacilhis ferrooxidans was purified 55-fold. Polyacrylamide gel electrophoresis of the most purified fraction showed only one major band; histochemical analysis showed that the ATPase activity was associated with this band. The pH optimum is 9–10.
C, Adapoe, M, Silver
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