Affinity gradients drive copper to cellular destinations

Lucia Banci, Ivano Bertini (), Simone Ciofi-Baffoni, Tatiana Kozyreva, Kairit Zovo and Peep Palumaa ()
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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

Nature, 2010, vol. 465, issue 7298, 645-648

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.

Date: 2010
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DOI: 10.1038/nature09018

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