Martin C Feiters et al 2009 J. Phys.: Conf. Ser. 190 012196 doi:10.1088/1742-6596/190/1/012196
Martin C Feiters1, Wolfram Meyer-Klaucke2, Alexander V Kostenko3, Alexander V Soldatov3, Catherine Leblanc4, Gurvan Michel4, Philippe Potin4, Frithjof C Küpper5, Kaspar Hollenstein6, Kaspar P Locher6, Loes E Bevers7, Peter-Leon Hagedoorn7 and Wilfred R Hagen7
Show affiliationsWe compare aspects of biological X-ray absorption spectroscopy (XAS) studies of cations and anions, and report on some examples of anion binding in biological systems. Brown algae such as Laminaria digitata (oarweed) are effective accumulators of I from seawater, with tissue concentrations exceeding 50 mM, and the vanadate-containing enzyme haloperoxidase is implicated in halide accumulation. We have studied the chemical state of iodine and its biological role in Laminaria at the I K edge, and bromoperoxidase from Ascophyllum nodosum (knotted wrack) at the Br K edge. Mo is essential for many forms of life; W only for certain archaea, such as Archaeoglobus fulgidus and the hyperthermophilic archaeon Pyrococcus furiosus, and some bacteria. The metals are bound and transported as their oxo-anions, molybdate and tungstate, which are similar in size. The transport protein WtpA from P. furiosus binds tungstate more strongly than molybdate, and is related in sequence to Archaeoglobus fulgidus ModA, of which a crystal structure is known. We have measured A. fulgidus ModA with tungstate at the W L3 (2p3/2) edge, and compared the results with the refined crystal structure. XAS studies of anion binding are feasible even if only weak interactions are present, are biologically relevant, and give new insights in the spectroscopy.
87.15.K- Molecular interactions; membrane-protein interactions
Issue 1 (2009)
Martin C Feiters et al 2009 J. Phys.: Conf. Ser. 190 012196
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