Letter/Communication
Structural Implications for Blue Protein Copper Centers from Electron Spin Resonance Spectra of Cu11S4 Chromophores
Journal of the American Chemical Society, Vol.99(15), pp.5189-5190
01 Jan 1977
PMID: 194943
Abstract
Current interest in copper(II)-sulfur bonding has been stimulated by the finding of the copper(II)-sulfur (cysteine) bond being involved in the copper centers in “blue” copper proteins. It has recently been shown that the intense blue coloration and high positive redox potentials in these proteins can be mimicked by simple inorganic compounds containing copper(II)-sulfur bonding. However, the origin of the anomalously small hyperfine(hf) coupling constants in the electron spin resonance (ESR) spectra of “blue” proteins is as yet uncertain. Several compounds containing copper(II)-sulfur bond(s) have been proposed as models for the “blue” copper centers, but they all show too large |A| and/or g|| values. Thus, the proposed spatial disposition of ligand atoms around the “blue” copper centers varies from flattened tetrahedral,11 trigonal-bipyramidal,12 and penta coordinated 13 to planar. The diversity of these models appears to result mainly from the paucity of pertinent ESR data, especially for tetrahedral copper(II) centers containing copper (II)-sulfur bonding. [1st paragraph]
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Details
- Title
- Structural Implications for Blue Protein Copper Centers from Electron Spin Resonance Spectra of Cu11S4 Chromophores
- Creators
- U Sakaguchi - University of British ColumbiaA W Addison - University of British Columbia
- Publication Details
- Journal of the American Chemical Society, Vol.99(15), pp.5189-5190
- Publisher
- Amer Chemical Soc
- Number of pages
- 2
- Resource Type
- Letter/Communication
- Language
- English
- Academic Unit
- Chemistry
- Identifiers
- 991022027636904721