Isolation and identification of an iron-oxidizing bacterium which can grow on tetrathionate medium and the properties of a tetrathionate- decomposing enzyme isolated from the bacterium

Tsuyoshi Sugio, Tadayoshi Kanao, Hirotaka Furukawa, Toru Nagasawa, Robert C. Blake

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Among 150 pure strains of iron-oxidizing bacteria obtained from natural environments, two strains, Funis 2-1 and OK1-50, had the ability to use potassium tetrathionate (K2S4O6) as a sole energy source for growth. Funis 2-1 was a gram-negative, rod-shaped, acidophilic iron- and sulfur-oxidizing chemolithotrophic bacterium and had the same cytochrome composition and mean G+C content of DNA as Thiobacillus ferrooxidans, indicating that the strain is T. ferrooxidans. A tetrathionate-decomposing enzyme that catalyzes the disproportionate metabolism of 4 tool of tetrathionate into 7 mol of thiosulfate and 2 tool of sulfate was located on the plasma membrane of K2S4O6-grown, but not Fe2+-grown Funis 2-1 cells. Washed intact cells and cell extracts prepared from Funis 2-1 cells grown on K2S4O6 medium supplemented with more than 11 mM FeSO4 did not show K2S4O6-decomposing enzyme activity. K2S4O6-decomposing enzyme was purified to homogeneity from K2S4O6-grown Funis 2-1 cells. The apparent molecular weight of this enzyme was estimated to be 50,000 by gel filtration, 50,000 by SDS-PAGE, and 49,600 using a time-of-flight mass spectrometer, indicating that the enzyme is monomeric. The enzyme was most active at pH 3.5 and 50°C and the activity was enhanced approximately 18 fold by a concentration of 200 mM of sulfate ion. The Michaelis constant of this enzyme for K2S4O6 was 0.73 mM.

Original languageEnglish
Pages (from-to)233-238
Number of pages6
JournalJournal of Fermentation and Bioengineering
Volume82
Issue number3
DOIs
Publication statusPublished - 1996

Fingerprint

Bacteria
Iron
Enzymes
Sulfates
Tetrathionic Acid
Thiosulfates
Thiobacillus
Enzyme activity
Mass spectrometers
Cell membranes
Cytochromes
Sulfur
Metabolism
Base Composition
Potassium
Cell Extracts
DNA
Gels
Gel Chromatography
Molecular weight

Keywords

  • chemolithotrophic bacterium
  • sulfur metabolism
  • tetrathionate-decomposing enzyme
  • Thiobacillus ferrooxidans

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Isolation and identification of an iron-oxidizing bacterium which can grow on tetrathionate medium and the properties of a tetrathionate- decomposing enzyme isolated from the bacterium. / Sugio, Tsuyoshi; Kanao, Tadayoshi; Furukawa, Hirotaka; Nagasawa, Toru; Blake, Robert C.

In: Journal of Fermentation and Bioengineering, Vol. 82, No. 3, 1996, p. 233-238.

Research output: Contribution to journalArticle

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N2 - Among 150 pure strains of iron-oxidizing bacteria obtained from natural environments, two strains, Funis 2-1 and OK1-50, had the ability to use potassium tetrathionate (K2S4O6) as a sole energy source for growth. Funis 2-1 was a gram-negative, rod-shaped, acidophilic iron- and sulfur-oxidizing chemolithotrophic bacterium and had the same cytochrome composition and mean G+C content of DNA as Thiobacillus ferrooxidans, indicating that the strain is T. ferrooxidans. A tetrathionate-decomposing enzyme that catalyzes the disproportionate metabolism of 4 tool of tetrathionate into 7 mol of thiosulfate and 2 tool of sulfate was located on the plasma membrane of K2S4O6-grown, but not Fe2+-grown Funis 2-1 cells. Washed intact cells and cell extracts prepared from Funis 2-1 cells grown on K2S4O6 medium supplemented with more than 11 mM FeSO4 did not show K2S4O6-decomposing enzyme activity. K2S4O6-decomposing enzyme was purified to homogeneity from K2S4O6-grown Funis 2-1 cells. The apparent molecular weight of this enzyme was estimated to be 50,000 by gel filtration, 50,000 by SDS-PAGE, and 49,600 using a time-of-flight mass spectrometer, indicating that the enzyme is monomeric. The enzyme was most active at pH 3.5 and 50°C and the activity was enhanced approximately 18 fold by a concentration of 200 mM of sulfate ion. The Michaelis constant of this enzyme for K2S4O6 was 0.73 mM.

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