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Article
Mercury Metallation of the Copper Protein Azurin and Structural Insight into Possible Heavy Metal Reactivity.
Journal of Inorganic Biochemistry
  • Anthony P Zampino, University of Akron Main Campus
  • Francesca M Masters, University of Akron Main Campus
  • Erika L Bladholm
  • Matthew J. Panzner, University of Akron Main Campus
  • Steven M Berry
  • Thomas C Leeper, University of Akron Main Campus
  • Christopher J Ziegler, University of Akron Main Campus
Document Type
Article
Publication Date
12-1-2014
Disciplines
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.
Citation Information
Anthony P Zampino, Francesca M Masters, Erika L Bladholm, Matthew J. Panzner, et al.. "Mercury Metallation of the Copper Protein Azurin and Structural Insight into Possible Heavy Metal Reactivity." Journal of Inorganic Biochemistry Vol. 141 (2014) p. 152 - 160
Available at: http://works.bepress.com/thomas_leeper/5/