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Localization, purification and properties of a tetrathionate hydrolase from Acidithiobacillus caldus
Umeå University, Faculty of Medicine, Department of Odontology.
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
2004 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 271, no 2, 272-280 p.Article in journal (Refereed) PublishedText
Abstract [en]

The moderately thermophilic bacterium Acidithiobacillus caldus is found in bacterial populations in many bioleaching operations throughout the world. This bacterium oxidizes elemental sulfur and other reduced inorganic sulfur compounds as the sole source of energy. The purpose of this study was to purify and characterize the tetrathionate hydrolase of A. caldus. The enzyme was purified 16.7-fold by one step chromatography using a SP Sepharose column. The purified enzyme resolved into a single band in 10% polyacrylamide gel, both under denaturing and native conditions. Its homogeneity was confirmed by N-terminal amino acid sequencing. Tetrathionate hydrolase was shown to be a homodimer with a molecular mass of 103 kDa (composed from two 52 kDa monomers). The purified enzyme had optimum activity at pH 3.0 and 40 degreesC and an isoelectric point of 9.8. The periplasmic localization of the enzyme was determined by differential fractionation of A. caldus cells. Detected products of the tetrathionate hydrolase reaction were thiosulfate and pentathionate as confirmed by RP-HPLC analysis. The activity of the purified enzyme was drastically enhanced by divalent metal ions.

Place, publisher, year, edition, pages
Hoboken: Wiley-Blackwell, 2004. Vol. 271, no 2, 272-280 p.
Keyword [en]
Acidithiobacillus caldus, tetrathionate hydrolase, protein purification, intracellular protein localization, reduced inorganic sulfur compounds
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-122188DOI: 10.1046/j.1432-1033.2003.03926.xISI: 000187958900005PubMedID: 14717695OAI: oai:DiVA.org:umu-122188DiVA: diva2:938531
Available from: 2016-06-17 Created: 2016-06-15 Last updated: 2016-06-17Bibliographically approved

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Bugaytsova, ZhannaLindström, E Börje
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Department of OdontologyDepartment of Molecular Biology (Faculty of Science and Technology)
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