Purification and characterization of a periplasmic thiosulfate dehydrogenase from the obligately autotrophic Thiobacillus sp. W5

A periplasmic thiosulfate dehydrogenase (EC 1.8.2.2) was purified to homogeneity from the neutrophilic, obligately chemolithoautotrophic Thiobacillus sp. W5. A five-step procedure resulted in an approximately 2,300-fold purification. The purified protein had a molecular mass of 120 +/- 3 kDa, as det...

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Veröffentlicht in:	Archives of microbiology 1996-12, Vol.166 (6), p.372-378
Hauptverfasser:	VISSER, J. M, DE JONG, G. A. H, ROBERTSON, L. A, KUENEN, J. G
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - isolation & purification Bacteriology Biological and medical sciences Cytochrome c Group - metabolism Electrophoresis, Polyacrylamide Gel Enzyme Inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Kinetics Metabolism. Enzymes Microbiology Oxidation-Reduction Oxidoreductases - antagonists & inhibitors Oxidoreductases - isolation & purification Oxidoreductases - metabolism Oxidoreductases Acting on Sulfur Group Donors Protein Conformation Pyridines - metabolism Spectrophotometry, Ultraviolet Substrate Specificity Sulfurtransferases Thiobacillus Thiobacillus - enzymology Thiosulfates - metabolism
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