Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7Å

Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7Å
J Inorg Biochem. 2013 Jul 16;128C:11-16
Authors: Panzner MJ, Bilinovich SM, Parker JA, Bladholm EL, Ziegler CJ, Berry SM, Leeper TC
Abstract
Multiple biophysical methods demonstrate that silver effectively metallates Pseudomonas aeruginosa apo-azurin in solution. X-ray crystallography of the silver-modified protein reveals that silver binds to azurin at the traditional copper mediated active site with nearly identical geometry. Cyclic voltammetry indicates that the silver adduct is redox inert. Our results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.
PMID: 23911566 [PubMed - as supplied by publisher]

Source: Journal of Inorganic Biochemistry - July 16, 2013 Category: Biochemistry Authors: Panzner MJ, Bilinovich SM, Parker JA, Bladholm EL, Ziegler CJ, Berry SM, Leeper TC Tags: J Inorg Biochem Source Type: research