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  • 1
    ISSN: 1432-072X
    Keywords: Tetrathionate Reductase ; Thiosulphate Reductase ; Anaerobic Respiration ; Cytoplasmic Membrane ; Enzyme Purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Solubilization of cytoplasmic membrane bound tetrathionate and thiosulphate reductase was accomplished without detergents by repeated extraction of a purified cytoplasmic membrane suspension with tert-amyl alcohol. On homokinetic sucrose gradients both solubilized reductase activities banded in single peaks in the same fractions. A sedimentation constant of 6.9 Svedbergs was calculated using catalase as indicator enzyme. Further purification was obtained on an electro focusing column. Again both reductase activities banded as a single peak in the same fractions. It can be concluded that both have an isoelectric point of 5.22. It was demonstrated on polyacrylamide gels that the peak fractions contained virtually one protein component, which catalyzes tetrathionate reduction as well as thiosulphate reduction. It was concluded that Proteus mirabilis has only one enzyme for both enzymatic functions. From polyacrylamide gel electrophoresis in 0.1% sodium dodecyl sulphate it appeared that this enzyme consists of two subunits with molecular weights of approx. 43 000 and 90 000 daltons. The complete enzyme has thus a molecular weight of approx. 133 000 daltons. Protein profiles of cytoplasmic membranes isolated after various growth conditions suggest that the smaller subunit of this enzyme is present after anaerobic growth in the presence of KNO3 in spite of repression of the complete enzyme under this growth condition.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 105 (1975), S. 135-142 
    ISSN: 1432-072X
    Keywords: Tetrathionate Reductase ; Trithionate Reductase ; Thiosulphate Reductase ; Sulphide Oxidation ; Anaerobic Respiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The reductase catalyzing the reduction of tetrathionate and thiosulphate in Proteus mirabilis is also concerned with the reduction of trithionate and the oxidation of sulphide. Tetrathionate is reduced to thiosulphate, thiosulphate to sulphite and sulphide, and trithionate is reduced to thiosulphate plus sulphite. The oxidation of sulphide in cell-free extracts proceeds most likely to polysulphanes or to elemental sulphur, depending on the conditions. The kinetics of the reduction of tetrathionate imply a simultaneous interaction of tetrathionate and thiosulphate on the reductase molecule. The reduction of tetrathionate is activated by thiosulphate causing a non-linear progress of this reaction. On the other hand the reduction of thiosulphate is completely blocked until tetrathionate has been depleted. The order of reduction in a mixture of thiosulphate and trithionate is imputed by the enzymatic constants of the reductase for both substrates. Therefore in cell-free extracts thiosulphate is reduced prior to trithionate and afterwards, when thiosulphate has been exhausted, trithionate and the produced thiosulphate are reduced simultaneously. Fast growing cells, however, reduce trithionate first since their intracellular redox potential is insulfficiently low to permit the reduction of any thiosulphate.
    Type of Medium: Electronic Resource
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