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 (25kDa), 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 sulfurgrown 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 aa3type cytochrome c oxidase. This is the first report to indicate that aa3-type cytochrome c oxidase catalyzed sulfite oxidation in A. ferrooxidans.
| Original language | English |
|---|---|
| Pages (from-to) | 2242-2247 |
| Number of pages | 6 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 74 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2010 |
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Keywords
- Aa-type cytochrome oxidase
- Acidithiobacillus ferrooxidans
- Bioleaching
- Sulfite oxidase
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Applied Microbiology and Biotechnology
- Analytical Chemistry
- Organic Chemistry
Cite this
Sulfite oxidation catalyzed by aa3-type cytochrome c oxidase in Acidithiobacillus ferrooxidans. / Sugio, Tsuyoshi; Ako, Ami; Takeuchi, Fumiaki.
In: Bioscience, Biotechnology and Biochemistry, Vol. 74, No. 11, 2010, p. 2242-2247.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Sulfite oxidation catalyzed by aa3-type cytochrome c oxidase in Acidithiobacillus ferrooxidans
AU - Sugio, Tsuyoshi
AU - Ako, Ami
AU - Takeuchi, Fumiaki
PY - 2010
Y1 - 2010
N2 - 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 (25kDa), 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 sulfurgrown 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 aa3type cytochrome c oxidase. This is the first report to indicate that aa3-type cytochrome c oxidase catalyzed sulfite oxidation in A. ferrooxidans.
AB - 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 (25kDa), 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 sulfurgrown 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 aa3type cytochrome c oxidase. This is the first report to indicate that aa3-type cytochrome c oxidase catalyzed sulfite oxidation in A. ferrooxidans.
KW - Aa-type cytochrome oxidase
KW - Acidithiobacillus ferrooxidans
KW - Bioleaching
KW - Sulfite oxidase
UR - http://www.scopus.com/inward/record.url?scp=78649787038&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78649787038&partnerID=8YFLogxK
U2 - 10.1271/bbb.100446
DO - 10.1271/bbb.100446
M3 - Article
C2 - 21071859
AN - SCOPUS:78649787038
VL - 74
SP - 2242
EP - 2247
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 11
ER -