Glutathione Reductase-Mediated Synthesis of Tellurium-Containing Nanostructures Exhibiting Antibacterial Properties
Author(s) -
Benoı̂t Pugin,
Fabián A. Cornejo,
Pablo Muñoz-Díaz,
Claudia Muñoz-Villagrán,
Joaquín I. Vargas-Pérez,
Felipe Arenas,
Claudio C. Vásquez
Publication year - 2014
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.02207-14
Subject(s) - glutathione , glutathione reductase , tellurium , nanostructure , chemistry , antibacterial activity , nanotechnology , enzyme , combinatorial chemistry , bacteria , biochemistry , materials science , biology , inorganic chemistry , glutathione peroxidase , genetics
Tellurium, a metalloid belonging to group 16 of the periodic table, displays very interesting physical and chemical properties and lately has attracted significant attention for its use in nanotechnology. In this context, the use of microorganisms for synthesizing nanostructures emerges as an eco-friendly and exciting approach compared to their chemical synthesis. To generate Te-containing nanostructures, bacteria enzymatically reduce tellurite to elemental tellurium. In this work, using a classic biochemical approach, we looked for a novel tellurite reductase from the Antarctic bacteriumPseudomonas sp. strain BNF22 and used it to generate tellurium-containing nanostructures. A new tellurite reductase was identified as glutathione reductase, which was subsequently overproduced inEscherichia coli . The characterization of this enzyme showed that it is an NADPH-dependent tellurite reductase, with optimum reducing activity at 30°C and pH 9.0. Finally, the enzyme was able to generate Te-containing nanostructures, about 68 nm in size, which exhibit interesting antibacterial properties againstE. coli , with no apparent cytotoxicity against eukaryotic cells.
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