Existence of a tungsten-binding protein in Acidithiobacillus ferrooxidans AP19-3

Tsuyoshi Sugio, Hiroyuki Kuwano, Yoshiko Hamago, Atsunori Negishi, Terunobu Maeda, Fumiaki Takeuchi, Kazuo Kamimura

Research output: Contribution to journalReview articlepeer-review

5 Citations (Scopus)


A tungsten-binding protein was purified from a plasma membrane preparation of the iron-oxidizing bacterium, Acidithiobacillus ferrooxidans AP19-3 in an electrophoretically homogenous state. The protein was composed of two subunits with apparent molecular masses of 12 and 20.7 kDa. The molecular mass of the native protein was estimated to be 26.4 kDa in the presence of 1.5% 1-o-octyl-D-glucopyranoside (OGL), indicating that the native tungsten-binding protein is a heterodimeric protein. The amounts of tungsten bound to 1 mg of plasma membranes of A. ferrooxidans AP19-3 and the purified tungsten-binding protein at pH 3.0 were 191 and 1506 μg, respectively. In contrast, the amounts of tungsten bound to 1 mg of albumin, aldolase, catalase, chymotrypsinogen A, ferritin, and ferredoxin at pH 3.0 were 13.1, 18.6, 12.8, 16.6, 11.4, and 6.1 μg, respectively. Incubation of the tungsten-binding protein for 1 h with 10 mM Na2WO4 plus 10 mM metal ion, such as NaVO3, Na2MoO4, CuSO4, NiSO4, MnSO4, CoSO4, or CdCl2, did not markedly affect the amount of tungsten bound to the tungsten-binding protein, suggesting that the protein specifically binds tungsten.

Original languageEnglish
Pages (from-to)378-382
Number of pages5
JournalJournal of Bioscience and Bioengineering
Issue number6
Publication statusPublished - 2004


  • Acidithiobacillus ferrooxidans
  • Heavy metal
  • Tungsten-binding protein

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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