Open AccessElectron paramagnetic resonance spectroscopy of Cu2+ in hen egg-white lysozyme.
Author(s) -
Clyde A. Hutchison,
David J. Singel,
Michael N. Hadad,
Marvin D. Kemple
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.9.5243
Subject(s) - electron paramagnetic resonance , lysozyme , tetragonal crystal system , crystallography , electron paramagnetic resonance spectroscopy , chemistry , spectroscopy , ion , paramagnetism , nuclear magnetic resonance , crystal structure , physics , condensed matter physics , biochemistry , organic chemistry , quantum mechanics
We have obtained the electron paramagnetic resonance spectrum of Cu2+ bound in a tetragonal single crystal of hen egg-white lysozyme. A part of this spectrum has been shown to originate from Cu2+ ions bound at the site designated as B by Teichberg et al. [Teichberg, V.I., Sharon, N., Moult, J., Smilansky, A. & Yonath, A. (1974) J. Mol. Biol. 87, 357-368]. The values of the spin hamiltonian parameters that describe this part of the spectrum are reported. The implications of these values with respect to the chemical nature and configuration of ligands are discussed. The other features of the spectrum are also described.