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Progress toward clonable inorganic nanoparticles.

Thomas W Ni1, Lucian C Staicu, Richard S Nemeth

  • 1Department of Chemistry, Colorado State University, Fort Collins, CO 80523, USA. ackerson@colostate.edu.

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|September 10, 2015
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Summary
This summary is machine-generated.

This study identifies glutathione reductase as a key enzyme produced by Pseudomonas moraviensis stanleyae for creating selenium nanoparticles. The enzyme facilitates selenite reduction and nanoparticle formation within the bacterium.

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Area of Science:

  • Microbiology
  • Biotechnology
  • Environmental Science

Background:

  • Pseudomonas moraviensis stanleyae, isolated from the selenium hyperaccumulator plant Stanleya pinnata, tolerates high selenium concentrations.
  • This bacterium produces intracellular selenium (Se) nanoparticles.

Purpose of the Study:

  • To identify the enzymes responsible for selenite reduction and Se nanoparticle formation in P. moraviensis stanleyae.
  • To characterize the Se nanoparticles and their formation process.

Main Methods:

  • Cellular electron tomography for nanoparticle structure analysis.
  • Protein mass spectrometry to identify candidate enzymes.
  • In vitro experiments with purified glutathione reductase.

Main Results:

  • Glutathione reductase homologues were identified as candidate enzymes for selenite reduction.
  • In vitro assays confirmed NADPH-dependent reduction of selenite to Se nanoparticles by glutathione reductase.
  • Nanoparticle size correlated with selenite concentration (5 nm at 1.0 μM to 50 nm at 100 μM).
  • Glutathione reductase appears to be retained within or entombed by the formed nanoparticles.

Conclusions:

  • Glutathione reductase is a key enzyme for bacterial Se nanoparticle biogenesis.
  • The enzyme exhibits characteristics of a self-clonable nanoparticle system, including ion reduction, retention, and size control.