Purification and some properties of a hydrogen sulfide-binding protein that is involved in sulfur oxidation of Thiobacillus ferrooxidans

Tsuyoshi Sugio, Hiroyuki Suzuki, Aya Oto, Kenji Inagaki, Hidehiko Tanaka, Tatsuo Tano

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

A hydrogen sulfide: ferric ion oxidoreductase (SFORase), which is crucial in sulfur oxidation of T. ferrooxidans AP19-3, oxidizes hydrogen sulfide with Fe3 +as an electron acceptor to give sulfite ion and Fe2 +. When washed intact cells of T. ferrooxidans AP19-3 were treated with hydrogen sulfide solution (100 mM) at pH 6.5 for 1 hr, a heat stable reduced sulfur containing protein, which serves as a reduced sulfur compound for purified SFORase to give sulfite, was formed in the plasma membrane of this strain. The protein, which can bind hydrogen sulfide reversibly, was solubilized from plasma membrane with 1% SDS and purified to an electrophoretically homogeneous state. We tentatively named the protein hydrogen sulfide-binding protein (SBP). SBP had an apparent molecular weight of 16, 000 in the presence of 1% SDS. One molecule of SBP had 4.5 molecules of iron and could bind 2.3 molecules of hydrogen sulfide. The hydrogen sulfide bound to SBP was oxidized by a purified SFORase to give sulfite ion, suggesting that SBP is involved in sulfur oxidation of this bacterium.

Original languageEnglish
Pages (from-to)2091-2097
Number of pages7
JournalAgricultural and Biological Chemistry
Volume55
Issue number8
DOIs
Publication statusPublished - 1991

Fingerprint

Acidithiobacillus ferrooxidans
Thiobacillus
Hydrogen Sulfide
hydrogen sulfide
Sulfur
Sulfides
Purification
binding proteins
sulfides
Carrier Proteins
sulfur
oxidation
Oxidation
Sulfites
Ions
ions
sulfites
oxidoreductases
Oxidoreductases
Cell membranes

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Purification and some properties of a hydrogen sulfide-binding protein that is involved in sulfur oxidation of Thiobacillus ferrooxidans. / Sugio, Tsuyoshi; Suzuki, Hiroyuki; Oto, Aya; Inagaki, Kenji; Tanaka, Hidehiko; Tano, Tatsuo.

In: Agricultural and Biological Chemistry, Vol. 55, No. 8, 1991, p. 2091-2097.

Research output: Contribution to journalArticle

Sugio, Tsuyoshi ; Suzuki, Hiroyuki ; Oto, Aya ; Inagaki, Kenji ; Tanaka, Hidehiko ; Tano, Tatsuo. / Purification and some properties of a hydrogen sulfide-binding protein that is involved in sulfur oxidation of Thiobacillus ferrooxidans. In: Agricultural and Biological Chemistry. 1991 ; Vol. 55, No. 8. pp. 2091-2097.
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AU - Tanaka, Hidehiko

AU - Tano, Tatsuo

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AB - A hydrogen sulfide: ferric ion oxidoreductase (SFORase), which is crucial in sulfur oxidation of T. ferrooxidans AP19-3, oxidizes hydrogen sulfide with Fe3 +as an electron acceptor to give sulfite ion and Fe2 +. When washed intact cells of T. ferrooxidans AP19-3 were treated with hydrogen sulfide solution (100 mM) at pH 6.5 for 1 hr, a heat stable reduced sulfur containing protein, which serves as a reduced sulfur compound for purified SFORase to give sulfite, was formed in the plasma membrane of this strain. The protein, which can bind hydrogen sulfide reversibly, was solubilized from plasma membrane with 1% SDS and purified to an electrophoretically homogeneous state. We tentatively named the protein hydrogen sulfide-binding protein (SBP). SBP had an apparent molecular weight of 16, 000 in the presence of 1% SDS. One molecule of SBP had 4.5 molecules of iron and could bind 2.3 molecules of hydrogen sulfide. The hydrogen sulfide bound to SBP was oxidized by a purified SFORase to give sulfite ion, suggesting that SBP is involved in sulfur oxidation of this bacterium.

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