Enzyme-Catalyzed in situ Synthesis of Temporally and Spatially Distinct CdSe Quantum Dots in Biological Backgrounds.

The cellular machinery of metal metabolism is capable of making a wide range of inorganic nanoparticles and quantum dots. Individual enzymes from these metabolic pathways are being identified with metal reducing activity, and some have been isolated for in situ particle formation and labeling. We previously identified a glutathione reductase like metalloid reductase (GRLMR) from Pseudomonas Moravenis stanleyae with a high affinity for the bioavailable selenium thiolate selenodiglutatione, and exhibiting NADPH-dependent reduction of selenodiglutathione to Se(0); initiating the growth of pure selenium metal nanoparticles. In this study, we demonstrate that the GRLMR enzyme can further reduce selenium to a Se(2-) oxidative state, which is capable of nucleating with Cd(2+) to rapidly form CdSe quantum dots. We show that GRLMR can outcompete background sources of cellular selenium reduction (such as glutathione) and can control the kinetics of quantum dot formation in complex media. The resulting particles are smaller diameter, with a distinguishingly shifted emission spectra and superior FWHM. This study indicates that there is great potential for using GRLMR to study and design enzymes capable of controlled biosynthesis of nanoparticles and quantum dots; paving the way for cellularly assembled nanoparticle-biosensors and reporters.