Aspects of structure and bonding in copper-amino acid complexes revealed by single-crystal EPR/ENDOR spectroscopy and density functional calculations.

ABSTRACT: This work deduces from a series of well-defined copper-doped amino acid crystals, relationships between structural features of the copper complexes, and ligand-bound proton hyperfine parameters. These were established by combining results from electron paramagnetic resonance (EPR)/electron-nuclear double resonance (ENDOR) studies, crystallography, and were further assessed by quantum mechanical (QM) calculations. A detailed evaluation of previous studies on Cu(2+) doped into alpha-glycine, triglycine sulfate, alpha-glycylglycine, and L-alanine crystals reveal correlations between geometric features of the copper sites and proton hyperfine couplings from amino-bound and carbon-bound hydrogens. Experimental variations in proton isotropic hyperfine coupling values (a(iso)) could be fit to cos

SUBMITTER: Colaneri MJ 

PROVIDER: S-EPMC2896622 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature