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Affinity gradients drive copper to cellular destinations

Author

Listed:
  • Lucia Banci

    (University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy)

  • Ivano Bertini

    (University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy)

  • Simone Ciofi-Baffoni

    (University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy)

  • Tatiana Kozyreva

    (University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy)

  • Kairit Zovo

    (Tallinn University of Technology, Akadeemia tee 15, 12618 Tallinn, Estonia)

  • Peep Palumaa

    (Tallinn University of Technology, Akadeemia tee 15, 12618 Tallinn, Estonia)

Abstract

Intracellular copper transport Copper is an essential trace element for eukaryotes and for most prokaryotes, but intracellular free copper must be strictly limited due to its toxic side effects. For this reason, complex systems for copper trafficking have evolved to satisfy cellular requirements while minimizing toxicity. In this paper, the authors used mass spectrometry to measure the apparent Cu(I)-binding affinities for a representative set of intracellular copper proteins involved in enzymatic redox catalysis, in copper trafficking to and within various cellular compartments, and in copper storage. The resulting thermodynamic data indicate that copper is drawn to the enzymes that require it by passing from one copper protein site to another, exploiting gradients of increasing copper-binding affinity.

Suggested Citation

  • Lucia Banci & Ivano Bertini & Simone Ciofi-Baffoni & Tatiana Kozyreva & Kairit Zovo & Peep Palumaa, 2010. "Affinity gradients drive copper to cellular destinations," Nature, Nature, vol. 465(7298), pages 645-648, June.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7298:d:10.1038_nature09018
    DOI: 10.1038/nature09018
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    Cited by:

    1. Zhenxiang Zhao & Melissa Y. Lucero & Shengzhang Su & Eric J. Chaney & Jiajie Jessica Xu & Michael Myszka & Jefferson Chan, 2025. "Activity-based sensing reveals elevated labile copper promotes liver aging via hepatic ALDH1A1 depletion," Nature Communications, Nature, vol. 16(1), pages 1-12, December.

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