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Berlin Brandenburg

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  • 1
    Language: English
    In: Geochimica et Cosmochimica Acta, Jan 15, 2014, Vol.125, p.519(9)
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.gca.2013.10.010 Byline: Christian von Sperber, Hajo Kries, Federica Tamburini, Stefano M. Bernasconi, Emmanuel Frossard Abstract: Plants and microorganisms under phosphorus (P) stress release extracellular phosphatases as a strategy to acquire inorganic phosphate (P.sub.i). These enzymes catalyze the hydrolysis of phosphoesters leading to a release of P.sub.i. During the enzymatic hydrolysis an isotopic fractionation (I[micro]) occurs leaving an imprint on the oxygen isotope composition of the released P.sub.i which might be used to trace phosphorus in the environment. Therefore, enzymatic assays with acid phosphatases from wheat germ and potato tuber and alkaline phosphatase from Escherichia coli were prepared in order to determine the oxygen isotope fractionation caused by these enzymes. Adenosine 5' monophosphate and glycerol phosphate were used as substrates. The oxygen isotope fractionation caused by acid phosphatases is 20-30a[degrees] smaller than for alkaline phosphatases, resulting in a difference of 5-7.5a[degrees] in [delta].sup.18O of P.sub.i depending on the enzyme. We attribute the enzyme dependence of the isotopic fractionation to distinct reaction mechanisms of the two types of phosphatases. The observed difference is large enough to distinguish between the two enzymatic processes in environmental samples. These findings show that the oxygen isotope composition of P.sub.i can be used to trace different enzymatic processes, offering an analytical tool that might contribute to a better understanding of the P-cycle in the environment. Article History: Received 2 May 2013; Accepted 6 October 2013 Article Note: (miscellaneous) Associate editor: Jon Chorover
    Keywords: Adenosine ; Glycerol ; Enzymes ; Phosphates ; Enzymology ; Hydrolysis
    ISSN: 0016-7037
    Source: Cengage Learning, Inc.
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