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

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


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
Issue number39
StatePublished - Oct 7 2009
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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