This work was supported by the University of Houston and the American Cyanamid (Faculty Research Award to J. P. G.). The authors express their gratitude to Prof. R. S. Czernuszewicz and G. Fraczkiewicz (University of Houston) for the resonance Raman spectra, and Mr. V. Kurchev for assistance in acquiring the EPR spectra.
Novel Biological Copper Proteins through Anion Addition to the Mutant Met121Gly of Pseudomonas aeruginosa Azurin†
Article first published online: 22 DEC 2003
Copyright © 1995 by VCH Verlagsgesellschaft mbH, Germany
Angewandte Chemie International Edition in English
Volume 34, Issue 15, pages 1622–1624, August 18, 1995
How to Cite
Vidakovic, M. and Germanas, J. P. (1995), Novel Biological Copper Proteins through Anion Addition to the Mutant Met121Gly of Pseudomonas aeruginosa Azurin. Angew. Chem. Int. Ed. Engl., 34: 1622–1624. doi: 10.1002/anie.199516221
- Issue published online: 22 DEC 2003
- Article first published online: 22 DEC 2003
- Manuscript Received: 24 JAN 1995
- copper compounds;
- EPR spectroscopy;
- Raman spectroscopy
Azide, cyanide, and thiocyanate are the anions that, on addition to a variant produced by site-directed mutagenesis, Met121Gly, of Pseudomonas aeruginosa azurin, produce unprecedented copper proteins with markedly different spectroscopic properties. This ability to generate ligand-accessible metal centers in coordinatively saturated metalloproteins by directed mutagenesis might possibly bring the synthesis of metalloproteins that can be used as ion sensors a step nearer.