NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine

Michal S. Shoshan; Deborah E. Shalev; Wencke Adriaens; Maarten A. G. Merkx; Tilman M. Hackeng; Edit Y. Tshuva

doi:10.1039/c1cc11600b

NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine

Michal S. Shoshan, Deborah E. Shalev, Wencke Adriaens, Maarten A. G. Merkx, Tilman M. Hackeng, Edit Y. Tshuva^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH similar to 3.0 and similar to 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH similar to 8.5. This suggests a possible role of Met in metal transport.

Original language	English
Pages (from-to)	6407-6409
Journal	Chemical Communications
Volume	47
Issue number	22
DOIs	https://doi.org/10.1039/c1cc11600b
Publication status	Published - 2011

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title = "NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine",

abstract = "The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH similar to 3.0 and similar to 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH similar to 8.5. This suggests a possible role of Met in metal transport.",

author = "Shoshan, {Michal S.} and Shalev, {Deborah E.} and Wencke Adriaens and Merkx, {Maarten A. G.} and Hackeng, {Tilman M.} and Tshuva, {Edit Y.}",

year = "2011",

doi = "10.1039/c1cc11600b",

language = "English",

volume = "47",

pages = "6407--6409",

journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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T1 - NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine

AU - Shoshan, Michal S.

AU - Shalev, Deborah E.

AU - Adriaens, Wencke

AU - Merkx, Maarten A. G.

AU - Hackeng, Tilman M.

AU - Tshuva, Edit Y.

PY - 2011

Y1 - 2011

N2 - The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH similar to 3.0 and similar to 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH similar to 8.5. This suggests a possible role of Met in metal transport.

AB - The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH similar to 3.0 and similar to 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH similar to 8.5. This suggests a possible role of Met in metal transport.

U2 - 10.1039/c1cc11600b

DO - 10.1039/c1cc11600b

M3 - Article

C2 - 21552638

SN - 1359-7345

VL - 47

SP - 6407

EP - 6409

JO - Chemical Communications

JF - Chemical Communications

IS - 22

ER -

NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine

Abstract

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