Electron paramagnetic resonance spectroscopic study of copper hopping in doped bis(L-histidinato)cadmium dihydrate.

ABSTRACT: Electron paramagnetic resonance (EPR) spectroscopy was used to study Cu(II) dynamic behavior in a doped biological model crystal, bis(L-histidinato)cadmium dihydrate, in order to gain better insight into copper site stability in metalloproteins. Temperature-dependent changes in the low temperature X-band EPR spectra became visible around 100 K and continued up to room temperature. The measured 298 K g-tensor (principal values: 2.17, 2.16, 2.07) and copper hyperfine coupling tensor (principal values: -260, -190, -37 MHz) were similar to the average of the 77 K tensor values pertaining to two neighboring histidine binding sites. The observed temperature dependence was interpreted using Anderson's theory of motional narrowing, where the magnetic parameters for the different states are average

SUBMITTER: Colaneri MJ 

PROVIDER: S-EPMC3740127 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature