Low temperature 65Cu NMR spectroscopy of the Cu+ site in azurin

Andrew S. Lipton, Robert W. Heck, Wibe A. De Jong, Amy R. Gao, Xiongjian Wu, Adrienne Roehrich, Gerard S. Harbison, Paul D. Ellis

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Abstract

65Cu central-transition NMR spectroscopy of the blue copper protein azurin in the reduced Cu(I) state, conducted at 18.8 T and 10 K, gave a strongly second order quadrupole perturbed spectrum, which yielded a 65Cu quadrupole coupling constant of ±71.2 ± 1 MHz, corresponding to an electric field gradient of ±1.49 atomic units at the copper site, and an asymmetry parameter of approximately 0.2. Quantum chemical calculations employing second order Møller-Plesset perturbation theory and large basis sets successfully reproduced these experimental results. Sensitivity and relaxation times were quite favorable, suggesting that NMR may be a useful probe of the electronic state of copper sites in proteins.

Original languageEnglish (US)
Pages (from-to)13992-13999
Number of pages8
JournalJournal of the American Chemical Society
Volume131
Issue number39
DOIs
Publication statusPublished - Oct 7 2009

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Lipton, A. S., Heck, R. W., De Jong, W. A., Gao, A. R., Wu, X., Roehrich, A., ... Ellis, P. D. (2009). Low temperature 65Cu NMR spectroscopy of the Cu+ site in azurin. Journal of the American Chemical Society, 131(39), 13992-13999. https://doi.org/10.1021/ja901308v