VonSperberKriesTamburiniEtAl2014

Référence

von Sperber, C., Kries, H., Tamburini, F., Bernasconi, S.M., Frossard, E. (2014) The effect of phosphomonoesterases on the oxygen isotope composition of phosphate. Geochimica et Cosmochimica Acta, 125:519-527. (Scopus )

Résumé

Plants and microorganisms under phosphorus (P) stress release extracellular phosphatases as a strategy to acquire inorganic phosphate (Pi). These enzymes catalyze the hydrolysis of phosphoesters leading to a release of Pi. During the enzymatic hydrolysis an isotopic fractionation (ε) occurs leaving an imprint on the oxygen isotope composition of the released Pi 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 20-30‰ smaller than for alkaline phosphatases, resulting in a difference of 5-7.5‰ in δ18O of Pi 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 Pi 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. © 2013 Elsevier Ltd.

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@ARTICLE { VonSperberKriesTamburiniEtAl2014,
    AUTHOR = { von Sperber, C. and Kries, H. and Tamburini, F. and Bernasconi, S.M. and Frossard, E. },
    TITLE = { The effect of phosphomonoesterases on the oxygen isotope composition of phosphate },
    JOURNAL = { Geochimica et Cosmochimica Acta },
    YEAR = { 2014 },
    VOLUME = { 125 },
    PAGES = { 519-527 },
    NOTE = { cited By 36 },
    ABSTRACT = { Plants and microorganisms under phosphorus (P) stress release extracellular phosphatases as a strategy to acquire inorganic phosphate (Pi). These enzymes catalyze the hydrolysis of phosphoesters leading to a release of Pi. During the enzymatic hydrolysis an isotopic fractionation (ε) occurs leaving an imprint on the oxygen isotope composition of the released Pi 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 20-30‰ smaller than for alkaline phosphatases, resulting in a difference of 5-7.5‰ in δ18O of Pi 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 Pi 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. © 2013 Elsevier Ltd. },
    AFFILIATION = { Institute of Agricultural Sciences, ETH Zurich, Eschikon 33, CH-8315 Lindau, Switzerland; Laboratory of Organic Chemistry, ETH Zurich, ETH Hönggerberg, CH-8093 Zurich, Switzerland; Geological Institute, ETH Zurich, Sonneggstrasse 5, CH-8092 Zurich, Switzerland },
    DOCUMENT_TYPE = { Article },
    DOI = { 10.1016/j.gca.2013.10.010 },
    SOURCE = { Scopus },
    URL = { https://www.scopus.com/inward/record.uri?eid=2-s2.0-84888420404&doi=10.1016%2fj.gca.2013.10.010&partnerID=40&md5=8a0e3cbbbfcdccce3d11d1088c320211 },
}

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