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 language | English |
|---|---|
| Pages (from-to) | 152-160 |
| Number of pages | 9 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 82 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 1 2018 |
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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
Cite this
Characterization of tetrathionate hydrolase from the marine acidophilic sulfuroxidizing bacterium, Acidithiobacillus thiooxidans strain SH. / Kanao, Tadayoshi; Onishi, Moe; Kajitani, Yasuyuki; Hashimoto, Yuki; Toge, Tatsuya; Kikukawa, Hiroshi; Kamimura, Kazuo.
In: Bioscience, Biotechnology and Biochemistry, Vol. 82, No. 1, 01.01.2018, p. 152-160.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Characterization of tetrathionate hydrolase from the marine acidophilic sulfuroxidizing bacterium, Acidithiobacillus thiooxidans strain SH
AU - Kanao, Tadayoshi
AU - Onishi, Moe
AU - Kajitani, Yasuyuki
AU - Hashimoto, Yuki
AU - Toge, Tatsuya
AU - Kikukawa, Hiroshi
AU - Kamimura, Kazuo
PY - 2018/1/1
Y1 - 2018/1/1
N2 - 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.
AB - 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.
KW - Dissimilatory sulfur-oxidation
KW - Marine acidophilic bacterium
KW - Tetrathionate hydrolase
UR - http://www.scopus.com/inward/record.url?scp=85040813809&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85040813809&partnerID=8YFLogxK
U2 - 10.1080/09168451.2017.1415128
DO - 10.1080/09168451.2017.1415128
M3 - Article
C2 - 29303046
AN - SCOPUS:85040813809
VL - 82
SP - 152
EP - 160
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 1
ER -