Molybdenum Metabolism in Plants

Authors

  • W. Zimmer,

    1. Fraunhofer Institut für Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
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  • R. Mendel

    Corresponding author
    1. Botanisches Institut, Technische Universität Braunschweig, Germany
      Botanisches Institut Technische Universität Braunschweig HumboldtstraBe 1 D-38106 Braunschweig Germany E-mail: r.mendel@tu-bs.de
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Botanisches Institut Technische Universität Braunschweig HumboldtstraBe 1 D-38106 Braunschweig Germany E-mail: r.mendel@tu-bs.de

Abstract

Abstract: Among the micronutrients essential for plant growth and for microsymbionts, Mo is required in minute amounts. However, since Mo is often sequestered by Fe- or Al-oxihydrox-ides, especially in acidic soils, the concentration of the water-soluble molybdate anion available for uptake by plants may be limiting for the plant, even when the total Mo content of the soil is sufficient. In contrast to bacteria, no specific molybdenum uptake system is known for plants, but since molybdate and sulfate behave similarly and have similar structure, uptake of molybdate could be mediated unspecifically by one of the sulfate transporters. Transport into the different plant organs proceeds via xylem and phloem. A pterin-bound molybdenum is the cofactor of important plant enzymes involved in redox processes: nitrate reductase, xanthine dehydrogenase, aIdehyde oxidase, and probably sulfite oxidase. Biosynthesis of the molybdenum cofactor (Moco) starts with a guanosine-X-phos-phate. Subsequently, a sulfur-free pterin is synthesized, sulfur is added, and finally molybdenum is incorporated. In addition to the molybdopterin enzymes, small molybdopterin binding proteins without catalytic function are known and are probably involved in the storage of Moco. In symbiotic systems the nitrogen supply of the host plant is strongly influenced by the availability of Mo in soil, since both bacterial nitrogenase and NADPH-dependent nitrate reductase of mycorrhizal fungi are Mo enzymes.

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