Abstract
Thiosulfate dehydrogenase is known to play a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans. Enzyme activity measured using ferricyanide as the electron acceptor was detected in cell extracts of A. ferrooxidans ATCC 23270 grown on tetrathionate or sulfur, but no activity was detected in ferrous iron-grown cells. The enzyme was enriched 63-fold from cell extracts of tetrathionate-grown cells. Maximum enzyme activity (13.8 U mg-1) was observed at pH 2.5 and 70°C. The end product of the enzyme reaction was tetrathionate. The enzyme reduced neither ubiquinone nor horse heart cytochrome c, which serves as an electron acceptor. A major protein with a molecular mass of~25 kDa was detected in the partially purified preparation. Heme was not detected in the preparation, according to the results of spectroscopic analysis and heme staining. The open reading frame of AFE_0042 was identified by BLAST by using the N-terminal amino acid sequence of the protein. The gene was found within a region that was previously noted for sulfur metabolismrelated gene clustering. The recombinant protein produced in Escherichia coli had a molecular mass of~25 kDa and showed thiosulfate dehydrogenase activity, with maximum enzyme activity (6.5 U mg-1) observed at pH 2.5 and 50°C.
| Original language | English |
|---|---|
| Pages (from-to) | 113-120 |
| Number of pages | 8 |
| Journal | Applied and Environmental Microbiology |
| Volume | 79 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 2013 |
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ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Food Science
- Biotechnology
- Ecology
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Tetrathionate-forming thiosulfate dehydrogenase from the acidophilic, chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans. / Kikumoto, Mei; Nogami, Shohei; Kanao, Tadayoshi; Takada, Jun; Kamimura, Kazuo.
In: Applied and Environmental Microbiology, Vol. 79, No. 1, 01.2013, p. 113-120.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Tetrathionate-forming thiosulfate dehydrogenase from the acidophilic, chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans
AU - Kikumoto, Mei
AU - Nogami, Shohei
AU - Kanao, Tadayoshi
AU - Takada, Jun
AU - Kamimura, Kazuo
PY - 2013/1
Y1 - 2013/1
N2 - Thiosulfate dehydrogenase is known to play a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans. Enzyme activity measured using ferricyanide as the electron acceptor was detected in cell extracts of A. ferrooxidans ATCC 23270 grown on tetrathionate or sulfur, but no activity was detected in ferrous iron-grown cells. The enzyme was enriched 63-fold from cell extracts of tetrathionate-grown cells. Maximum enzyme activity (13.8 U mg-1) was observed at pH 2.5 and 70°C. The end product of the enzyme reaction was tetrathionate. The enzyme reduced neither ubiquinone nor horse heart cytochrome c, which serves as an electron acceptor. A major protein with a molecular mass of~25 kDa was detected in the partially purified preparation. Heme was not detected in the preparation, according to the results of spectroscopic analysis and heme staining. The open reading frame of AFE_0042 was identified by BLAST by using the N-terminal amino acid sequence of the protein. The gene was found within a region that was previously noted for sulfur metabolismrelated gene clustering. The recombinant protein produced in Escherichia coli had a molecular mass of~25 kDa and showed thiosulfate dehydrogenase activity, with maximum enzyme activity (6.5 U mg-1) observed at pH 2.5 and 50°C.
AB - Thiosulfate dehydrogenase is known to play a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans. Enzyme activity measured using ferricyanide as the electron acceptor was detected in cell extracts of A. ferrooxidans ATCC 23270 grown on tetrathionate or sulfur, but no activity was detected in ferrous iron-grown cells. The enzyme was enriched 63-fold from cell extracts of tetrathionate-grown cells. Maximum enzyme activity (13.8 U mg-1) was observed at pH 2.5 and 70°C. The end product of the enzyme reaction was tetrathionate. The enzyme reduced neither ubiquinone nor horse heart cytochrome c, which serves as an electron acceptor. A major protein with a molecular mass of~25 kDa was detected in the partially purified preparation. Heme was not detected in the preparation, according to the results of spectroscopic analysis and heme staining. The open reading frame of AFE_0042 was identified by BLAST by using the N-terminal amino acid sequence of the protein. The gene was found within a region that was previously noted for sulfur metabolismrelated gene clustering. The recombinant protein produced in Escherichia coli had a molecular mass of~25 kDa and showed thiosulfate dehydrogenase activity, with maximum enzyme activity (6.5 U mg-1) observed at pH 2.5 and 50°C.
UR - http://www.scopus.com/inward/record.url?scp=84871884927&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84871884927&partnerID=8YFLogxK
U2 - 10.1128/AEM.02251-12
DO - 10.1128/AEM.02251-12
M3 - Article
C2 - 23064330
AN - SCOPUS:84871884927
VL - 79
SP - 113
EP - 120
JO - Applied and Environmental Microbiology
JF - Applied and Environmental Microbiology
SN - 0099-2240
IS - 1
ER -