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Mercury Metallated Pseudomonas aeruginosa Azurin at 1.54 AMercury Metallated Pseudomonas aeruginosa Azurin at 1.54 A
Structural highlights
FunctionAZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. Publication Abstract from PubMedMercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5A 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. Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity.,Zampino AP, Masters FM, Bladholm EL, Panzner MJ, Berry SM, Leeper TC, Ziegler CJ J Inorg Biochem. 2014 Dec;141:152-60. doi: 10.1016/j.jinorgbio.2014.09.003. Epub , 2014 Sep 16. PMID:25265377[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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