<rdf:RDF xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dct="http://purl.org/dc/terms/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#">
  <rdf:Description rdf:about="https://doi.org/10.1017/qpb.2025.4">
    <dct:isReferencedBy>OPENAIRE</dct:isReferencedBy>
    <dct:isReferencedBy>OpenAire</dct:isReferencedBy>
    <dct:isReferencedBy>DOAJ</dct:isReferencedBy>
    <dct:isReferencedBy>Crossref</dct:isReferencedBy>
    <dct:isReferencedBy>Europe PubMed Central</dct:isReferencedBy>
    <dct:isReferencedBy>PubMed Central</dct:isReferencedBy>
    <dct:isPartOf>Quantitative Plant Biology</dct:isPartOf>
    <dct:license>Open Access</dct:license>
    <dct:created>2025-04-02</dct:created>
    <dc:description>Abstract    &lt;p&gt;The micronutrient zinc (Zn) is often poorly available but toxic when present in excess, so a tightly controlled Zn homoeostasis network operates in all organisms. This review summarizes our present understanding of plant Zn homoeostasis. In Arabidopsis, about 1,900 Zn-binding metalloproteins require Zn as a cofactor. Abundant Zn metalloproteins reside in plastids, mitochondria and peroxisomes, emphasizing the need to address how Zn reaches these proteins. Apo&#65506;&#65408;&#65427;Zn metalloproteins do not acquire Zn2+ from a cytosolic pool of free cations, but instead through associative ligand exchange from Zn-buffering molecules. The importance of cytosolic thiols in Zn buffering suggests that, besides elevated Zn influx, a more oxidized redox state is also predicted to cause elevated labile-bound Zn levels, consistent with the suppression of a Zn deficiency marker under oxidative stress. Therefore, we consider a broadened physiological scope in plants for a possible signalling role of Zn2+, experimentally supported only in animals to date.&lt;/p</dc:description>
    <dc:subject>zinc transporter</dc:subject>
    <dc:subject>QK1-989</dc:subject>
    <dc:subject>metal homeostasis</dc:subject>
    <dc:subject>Botany</dc:subject>
    <dc:subject>metalloprotein</dc:subject>
    <dc:subject>Plant culture</dc:subject>
    <dc:subject>plant nutrition</dc:subject>
    <dc:subject>Review</dc:subject>
    <dc:subject>zinc sensor</dc:subject>
    <dc:subject>SB1-1110</dc:subject>
    <dc:creator>Ute Kr&#228;mer</dc:creator>
    <dc:date>2025-01-01</dc:date>
    <dc:type>journalpaper</dc:type>
    <dct:abstract>Abstract    &lt;p&gt;The micronutrient zinc (Zn) is often poorly available but toxic when present in excess, so a tightly controlled Zn homoeostasis network operates in all organisms. This review summarizes our present understanding of plant Zn homoeostasis. In Arabidopsis, about 1,900 Zn-binding metalloproteins require Zn as a cofactor. Abundant Zn metalloproteins reside in plastids, mitochondria and peroxisomes, emphasizing the need to address how Zn reaches these proteins. Apo&#65506;&#65408;&#65427;Zn metalloproteins do not acquire Zn2+ from a cytosolic pool of free cations, but instead through associative ligand exchange from Zn-buffering molecules. The importance of cytosolic thiols in Zn buffering suggests that, besides elevated Zn influx, a more oxidized redox state is also predicted to cause elevated labile-bound Zn levels, consistent with the suppression of a Zn deficiency marker under oxidative stress. Therefore, we consider a broadened physiological scope in plants for a possible signalling role of Zn2+, experimentally supported only in animals to date.&lt;/p</dct:abstract>
    <dc:title>Changing paradigms for the micronutrient zinc, a known protein cofactor, as a signal relaying also cellular redox state</dc:title>
    <dc:identifier>10.1017/qpb.2025.4</dc:identifier>
    <dct:references>https://doi.org/10.1017/qpb.2025.4</dct:references>
    <dct:relation>788380</dct:relation>
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