Interplay between glutathione, Atx1 and copper: X-ray absorption spectroscopy determination of Cu(I) environment in an Atx1 dimer

Poger, David, Fillaux, Clara, Miras, Roger, Crouzy, Serge, Delangle, Pascale, Mintz, Elisabeth, Den Auwer, Christophe and Ferrand, Michel (2008) Interplay between glutathione, Atx1 and copper: X-ray absorption spectroscopy determination of Cu(I) environment in an Atx1 dimer. Journal of Biological Inorganic Chemistry, 13 8: 1239-1248. doi:10.1007/s00775-008-0408-1


Author Poger, David
Fillaux, Clara
Miras, Roger
Crouzy, Serge
Delangle, Pascale
Mintz, Elisabeth
Den Auwer, Christophe
Ferrand, Michel
Title Interplay between glutathione, Atx1 and copper: X-ray absorption spectroscopy determination of Cu(I) environment in an Atx1 dimer
Journal name Journal of Biological Inorganic Chemistry   Check publisher's open access policy
ISSN 0949-8257
1432-1327
Publication date 2008-11-01
Sub-type Article (original research)
DOI 10.1007/s00775-008-0408-1
Volume 13
Issue 8
Start page 1239
End page 1248
Total pages 10
Place of publication Berlin / Heidelberg, Germany
Publisher Springer
Language eng
Subject 060112 Structural Biology (incl. Macromolecular Modelling)
029901 Biological Physics
Formatted abstract
X-ray absorption techniques have been used to characterise the primary coordination sphere of Cu(I) bound to glutathionate (GS−), to Atx1 and in Cu2I(GS−)2(Atx1)2, a complex recently proposed as the major form of Atx1 in the cytosol. In each complex, Cu(I) was shown to be triply coordinated. When only glutathione is provided, each Cu(I) is triply coordinated by sulphur atoms in the binuclear complex CuI 2(GS−)5, involving bridging and terminal thiolates. In the presence of Atx1 and excess of glutathione, under conditions where CuI 2(GS−)2(Atx1)2 is formed, each Cu(I) is triply coordinated by sulphur atoms. Given these constraints, there are two different ways for Cu(I) to bridge the Atx1 dimer: either both Cu(I) ions contribute to bridging the dimer, or only one Cu(I) ion is responsible for bridging, the other one being coordinated to two glutathione molecules. These two models are discussed as regards Cu(I) transfer to Ccc2a.
Keyword X-ray absorption spectroscopy
Metallochaperones
Metal transport
Copper
Glutathione
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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