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

M.S. Shosham; D.E. Shalev; W. Adriaens; M. Merkx; T.M. Hackeng; E.Y. Tshuva

doi:10.1039/C1CC11600B

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

M.S. Shosham, D.E. Shalev, W. Adriaens, M. Merkx, T.M. Hackeng, E.Y. Tshuva

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

6 Citations (Scopus)

Abstract

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

Original language	English
Pages (from-to)	6407-6409
Number of pages	3
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 3.0 and 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH 8.5. This suggests a possible role of Met in metal transport.",

author = "M.S. Shosham and D.E. Shalev and W. Adriaens and M. Merkx and T.M. Hackeng and E.Y. Tshuva",

year = "2011",

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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 - Shosham, M.S.

AU - Shalev, D.E.

AU - Adriaens, W.

AU - Merkx, M.

AU - Hackeng, T.M.

AU - Tshuva, E.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 3.0 and 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH 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 3.0 and 6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH 8.5. This suggests a possible role of Met in metal transport.

U2 - 10.1039/C1CC11600B

DO - 10.1039/C1CC11600B

M3 - Article

VL - 47

SP - 6407

EP - 6409

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

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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