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  • Title: Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin.
    Author: Vila AJ, Ramirez BE, Di Bilio AJ, Mizoguchi TJ, Richards JH, Gray HB.
    Journal: Inorg Chem; 1997 Sep 24; 36(20):4567-4570. PubMed ID: 11670122.
    Abstract:
    NMR spectra of paramagnetic Co(II) and Cu(II) derivatives of Pseudomonas aeruginosa His46Asp azurin have been investigated. In each derivative, assignment of hyperfine-shifted resonances outside the diamagnetic envelope of spectra recorded at 200 and 500 MHz confirms that the Asp carboxylate is coordinated to the paramagnetic metal center. The reduced paramagnetic shifts of the Cys112 proton resonances in Cu(II) and Co(II) His46Asp azurins compared to those of the corresponding wild type proteins indicate that metal-S(Cys) bonding is weakened in this mutant. The downfield shifts of the gamma-CH(2) of Met121 suggest a stronger interaction between the metal and the Met thioether group than is present in the wild type protein. Molecular modeling of the metal site structure indicates a distorted tetrahedral geometry with Asp46 (monodentate carboxylate), Cys112, and His117 equatorial ligands. In this structure, the metal ion is shifted 0.3 Å out of the O(Asp)S(Cys)N(His) trigonal plane toward Met121.
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