title: NMR hyperfine shifts in blue copper proteins: a quantum chemical investigation.
abstract: 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 approximately 4.7% of the overall approximately 860 ppm shift range). We also find interesting correlations between the hyperfine shifts 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.
authors.affiliation: Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
authors.forename: Yong
authors.initials: Y
authors.lastname: Zhang
authors.forename: Eric
authors.initials: E
authors.lastname: Oldfield
mesh_terms: D001400:Azurin / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods / Q000592:standards*; D008667:Metalloproteins / Q000737:chemistry*; D008956:Models, Chemical; D010940:Plant Proteins / Q000737:chemistry*; D010970:Plastocyanin / Q000737:chemistry*; D011789:Quantum Theory; D012015:Reference Standards
chemical_list: D001426:Bacterial Proteins; D008667:Metalloproteins; D010940:Plant Proteins; C017079:mauC protein, Methylobacterium extorquens; C012543:rusticyanin; D001400:Azurin; C003343:stellacyanin protein, plant; D010970:Plastocyanin