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Published May 22, 1996 | public
Journal Article

Electronic Spectroscopy of Gold(I) Pseudomonasaeruginosa Azurin Derivatives

Abstract

The trigonal (His_2Cys) coordination of blue copper sites in proteins favors Cu(I) over Cu(II), as reflected in the relatively high Cu^(II/I) reduction potentials; and the rigid polypeptide environment minimizes Cu^(II/I) nuclear reorganization, thereby facilitating long-range electron-transfer reactions with donor and acceptor molecules. Although blue Cu(II) sites exhibit rich spectroscopic and magnetic properties, the corresponding Cu(I) proteins do not; indeed, the methods that can be employed to investigate d^(10) metal sites are very limited. Because recent work has shown that Au(I) has geometry-sensitive d-p absorptions and emissions, we are using this 5d^(10) ion to probe ligand interactions in the Cu(I) sites of proteins. Here we report the electronic spectroscopy of Au(I)-substituted wild-type (WT) Pseudomonas aeruginosa azurin as well as the Au(I) derivative of a mutant in which the methionine at position 121 has been replaced with glycine (Met121Gly).

Additional Information

© 1996 American Chemical Society. Received August 9, 1995. We thank Angelo Di Bilio, Bo Malmström, Vinny Miskowski, and Jay Winkler for helpful discussions. This work was supported by the National Institutes of Health (DK19038).

Additional details

Created:
August 18, 2023
Modified:
October 23, 2023