Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans
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- T Sugio
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University, Japan.
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- W Mizunashi
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University, Japan.
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- K Inagaki
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University, Japan.
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- T Tano
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University, Japan.
書誌事項
- 公開日
- 1987-11
- 権利情報
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- https://journals.asm.org/non-commercial-tdm-license
- DOI
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- 10.1128/jb.169.11.4916-4922.1987
- 公開者
- American Society for Microbiology
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説明
<jats:p>A sulfur:ferric ion oxidoreductase that utilizes ferric ion (Fe3+) as an electron acceptor of elemental sulfur was purified from iron-grown Thiobacillus ferrooxidans to an electrophoretically homogeneous state. Under anaerobic conditions in the presence of Fe3+, the enzyme reduced 4 mol of Fe3+ with 1 mol of elemental sulfur to give 4 mol of Fe2+ and 1 mol of sulfite, indicating that it corresponds to a ferric ion-reducing system (T. Sugio, C. Domatsu, O. Munakata, T. Tano, and K. Imai, Appl. Environ. Microbiol. 49:1401-1406, 1985). Under aerobic conditions, sulfite, but not Fe2+, was produced during the oxidation of elemental sulfur by this enzyme because the Fe2+ produced was rapidly reoxidized chemically by molecular oxygen. The possibility that Fe3+ serves as an electron acceptor under aerobic conditions was ascertained by adding o-phenanthroline, which chelates Fe2+, to the reaction mixture. Sulfur:ferric ion oxidoreductase had an apparent molecular weight of 46,000, and it is composed of two identical subunits (Mr = 23,000) as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sulfur oxidation by this enzyme was absolutely dependent on the presence of reduced glutathione. The enzyme had an isoelectric point and a pH optimum at pH 4.6 and 6.5, respectively. Almost all the activity of sulfur:ferric ion oxidoreductase was observed in the osmotic shock fluid of the cells, suggesting that it was localized in the periplasmic space of the cells.</jats:p>
収録刊行物
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- Journal of Bacteriology
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Journal of Bacteriology 169 (11), 4916-4922, 1987-11
American Society for Microbiology