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

FEBS Letters

Kuenen, Gijs J²  Sorokin, Dimitry Yu¹  Robertson, Lesley A²  de Jong, Govardus A.H² 

[1] Institute of Microbiology, Russian Academy of Sciences, Prospect 60-let Octyabrya, 7/2, 117811 Moscow, Russia;Kluyver Institute of Biotechnology, Department of Microbiology and Enzymology, Julianalaan 67, 2628 BC Delft, The Netherlands

关键词: Sulfide dehydrogenase;    Sulfur metabolism;    Membrane protein;    Thiosulfate;    Alkaliphilic thiobacillus;   

DOI  :  10.1016/S0014-5793(98)00379-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown