Sulfite Oxidation Catalyzed by aa3-Type Cytochrome c Oxidase in Acidithiobacillus ferrooxidans
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- SUGIO Tsuyoshi
- Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
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- AKO Ami
- Faculty of Agriculture, Okayama University
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- TAKEUCHI Fumiaki
- Environmental Management Center, Okayama University
Bibliographic Information
- Other Title
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- Sulfite Oxidation Catalyzed by<i>aa</i><sub>3</sub>-Type Cytochrome<i>c</i>Oxidase in<i>Acidithiobacillus ferrooxidans</i>
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Abstract
Sulfite is produced as a toxic intermediate during Acidithiobacillus ferrooxidans sulfur oxidation. A. ferrooxidans D3-2, which posseses the highest copper bioleaching activity, is more resistant to sulfite than other A. ferrooxidans strains, including ATCC 23270. When sulfite oxidase was purified homogeneously from strain D3-2, the oxidized and reduced forms of the purified sulfite oxidase absorption spectra corresponded to those of A. ferrooxidans aa3-type cytochrome c oxidase. The confirmed molecular weights of the α-subunit (52.5 kDa), the β-subunit (25 kDa), and the γ-subunit (20 kDa) of the purified sulfite oxidase and the N-terminal amino acid sequences of the γ-subunit of sulfite oxidase (AAKKG) corresponded to those of A. ferrooxidans ATCC 23270 cytochrome c oxidase. The sulfite oxidase activities of the iron- and sulfur-grown A. ferrooxidans D3-2 were much higher than those cytochrome c oxidases purified from A. ferrooxidans strains ATCC 23270, MON-1 and AP19-3. The activities of sulfite oxidase purified from iron- and sulfur-grown strain D3-2 were completely inhibited by an antibody raised against a purified A. ferrooxidans MON-1 aa3-type cytochrome c oxidase. This is the first report to indicate that aa3-type cytochrome c oxidase catalyzed sulfite oxidation in A. ferrooxidans.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 74 (11), 2242-2247, 2010
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390001206479438080
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- NII Article ID
- 10027561458
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 10899760
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed