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Generation of Scalable, Metallic High-Aspect Ratio Nanocomposites in a Biological Liquid Medium
Published on: July 8, 2015
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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.
Nanoscale
|September 10, 2015
Summary
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.
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.
