Characterization of tetrathionate hydrolase from the marine acidophilic sulfuroxidizing bacterium, Acidithiobacillus thiooxidans strain SH

Tadayoshi Kanao, Moe Onishi, Yasuyuki Kajitani, Yuki Hashimoto, Tatsuya Toge, Hiroshi Kikukawa, Kazuo Kamimura

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Tetrathionate hydrolase (4THase), a key enzyme of the S4-intermediate (S4I) pathway, was partially purified from marine acidophilic bacterium, Acidithiobacillus thiooxidans strain SH, and the gene encoding this enzyme (SH-Tth) was identified. SH-Tth is a homodimer with a molecular mass of 97 ± 3 kDa, and contains a subunit 52 kDa in size. Enzyme activity was stimulated in the presence of 1 M NaCl, and showed the maximum at pH 3.0. Although 4THases from A. thiooxidans and the closely related Acidithiobacillus caldus strain have been reported to be periplasmic enzymes, SH-Tth seems to be localized on the outer membrane of the cell, and acts as a peripheral protein. Furthermore, both 4THase activity and SH-Tth proteins were detected in sulfur-grown cells of strain SH. These results suggested that SH-Tth is involved in elemental sulfur-oxidation, which is distinct from sulfur-oxidation in other sulfur-oxidizing strains such as thiooxidans and A. caldus.

Original languageEnglish
Pages (from-to)152-160
Number of pages9
JournalBioscience, Biotechnology and Biochemistry
Volume82
Issue number1
DOIs
Publication statusPublished - Jan 1 2018

Keywords

  • Dissimilatory sulfur-oxidation
  • Marine acidophilic bacterium
  • Tetrathionate hydrolase

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Characterization of tetrathionate hydrolase from the marine acidophilic sulfuroxidizing bacterium, Acidithiobacillus thiooxidans strain SH'. Together they form a unique fingerprint.

  • Cite this