Electron nuclear double resonance spectra of stellacyanin, a blue copper protein Academic Article uri icon

abstract

  • The1H,14N, and63.65Cu electron nuclear double resonances (ENDOR) of stellacyanin have been measured. This represents the first published observation of copper ENDOR in a protein. In confirmation of the results of Rist et al., the cupric ion must have a minimum of two nitrogenous ligands. The Cu hyperfine splitting (hfs) tensor and the quadrupole tensor have been determined, the first such complete characterization for a copper protein. The unusual Cu hyperfine tensor can be explained by assuming a flattened tetrahedral geometry, without assumption as to the nature of the coordinated ligands; the observation of large quadrupole couplings also appears to be an effect of geometry. The coordination of Cu in stellacyanin is discussed in terms of these results. © 1980, American Chemical Society. All rights reserved.

published proceedings

  • Journal of the American Chemical Society

author list (cited authors)

  • Roberts, J. E., Brown, T. G., Hoffman, B. M., & Peisach, J

citation count

  • 64

complete list of authors

  • Roberts, James E||Brown, Theodore G||Hoffman, Brian M||Peisach, Jack

publication date

  • January 1980