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

Matthew J. Panzner, Stephanie M. Bilinovich, Jillian A. Parker, Erika L. Bladholm, Christopher J. Ziegler, Steven M. Berry, Thomas C. Leeper

Research output: Contribution to journalArticle

3 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)11-16
Number of pages6
JournalJournal of Inorganic Biochemistry
Volume128
DOIs
StatePublished - Aug 6 2013

Keywords

  • Azurin
  • Crystallography
  • NMR
  • Silver ion

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