NMR hyperfine shifts in blue copper proteins: A quantum chemical investigation

Yong Zhang, Eric Oldfield

Research output: Contribution to journalArticlepeer-review


We present the results of the first quantum chemical investigations of 1H NMR hyperfine shifts in the blue copper proteins (BCPs): amicyanin, azurin, pseudoazurin, plastocyanin, stellacyanin, and rusticyanin. We find that very large structural models that incorporate extensive hydrogen bond networks, as well as geometry optimization, are required to reproduce the experimental NMR hyperfine shift results, the best theory vs experiment predictions having R2 = 0.94, a slope = 1.01, and a SD = 40.5 ppm (or ∼4.7% of the overall ∼860 ppm shift range). We also find interesting correlations between the hyperfine shirts and the bond and ring critical point properties computed using atoms-in-molecules theory, in addition to finding that hyperfine shifts can be well-predicted by using an empirical model, based on the geometry-optimized structures, which in the future should be of use in structure refinement.

Original languageEnglish (US)
Pages (from-to)3814-3823
Number of pages10
JournalJournal of the American Chemical Society
Issue number12
StatePublished - Mar 26 2008

ASJC Scopus subject areas

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


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