Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria

Extracts of the alkaliphilic sulfur-oxidizing autotroph strain AL3 contained sulfide:cytochrome c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted...

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Bibliographic Details
Published in:FEBS letters 1998-05, Vol.427 (1), p.11-14
Main Authors: Sorokin, Dimitry Yu, de Jong, Govardus A.H, Robertson, Lesley A, Kuenen, Gijs J
Format: Article
Language:English
Subjects:
Alkaliphilic thiobacillus
Cytochrome c Group - isolation & purification
Membrane protein
Oxidation-Reduction
Oxidoreductases - isolation & purification
Sulfide dehydrogenase
Sulfides - metabolism
Sulfur metabolism
Thiobacillus - enzymology
Thiobacillus - metabolism
Thiosulfate
Thiosulfates - metabolism
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Summary:Extracts of the alkaliphilic sulfur-oxidizing autotroph strain AL3 contained sulfide:cytochrome c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted in an enzyme that catalyzed sulfide oxidation with horse heart cytochrome c. This enzyme was a 41 kDa protein containing heme c 554. The optimum pH of the membrane bound enzyme was 9.0, but after extraction this fell to 8.0. The enzyme catalyzed a single electron oxidation of HS −. Hydrosulfide radical is therefore the most probable product.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(98)00379-2