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.
Original language | English (US) |
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Pages (from-to) | 825-829 |
Number of pages | 5 |
Journal | Journal of the American Chemical Society |
Volume | 102 |
Issue number | 2 |
DOIs | |
State | Published - Jan 1980 |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry