Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity

Anthony P. Zampino, Francesca M. Masters, Erika L. Bladholm, Matthew J. Panzner, Steven M. Berry, Thomas C. Leeper, Christopher J. Ziegler

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Mercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5 Å of mercury(II) metallated azurin confirms the coordination of mercury at the copper binding active site and a second surface site. These findings are further validated by NMR, Matrix-assisted laser desorption/ionization spectrometry (MALDI), and UV-visible spectroscopic methods indicating copper displacement from the wild-type protein. Bioinformatic analysis has identified homologous human protein domains computationally, and compared them to the structure of azurin, providing a model for human mercury interactions. Study of the mercury-azurin adduct, in combination with other known examples of protein-heavy metal interactions, could provide further insight into the chemical mechanisms of toxicological interactions, leading toward a global understanding of the biological speciation of toxic heavy metals.

Original languageEnglish (US)
Pages (from-to)152-160
Number of pages9
JournalJournal of Inorganic Biochemistry
Volume141
DOIs
StatePublished - Dec 2014

Keywords

  • Azurin
  • Bioinformatics
  • MALDI
  • Mercury
  • NMR
  • X-ray structure

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