Fe(III) reduction during pyruvate fermentation by Desulfotomaculum reducens strain MI-1.

Desulfotomaculum reducens MI-1 is a Gram-positive, sulfate-reducing bacterium also capable of reducing several metals, among which is Fe(III). Very limited knowledge is available on the potential mechanism(s) of metal reduction among Gram-positive bacteria, despite their preponderance in the microbial communities that inhabit some inhospitable environments (e.g., thermal or hyperthermal ecosystems, extreme pH or salinity environments, heavy metal or radionuclide contaminated sediments). Here, we show that in the presence of pyruvate, this micro-organism is capable of reducing both soluble Fe(III)-citrate and solid-phase hydrous ferric oxide, although growth is sustained by pyruvate fermentation rather than Fe(III) respiration. Despite the fact that Fe(III) reduction does not support direct energy conservation, D. reducens uses it as a complementary means of discarding excess reducing equivalent after H2 accumulation in the culture headspace renders proton reduction unfavorable. Thus, Fe(III) reduction permits the oxidation of greater amounts of pyruvate than fermentation alone. Fe(III) reduction by D. reducens is mediated by a soluble electron carrier, most likely riboflavin. Additionally, an intracellular electron storage molecule acts as a capacitor and accumulates electrons during pyruvate oxidation for slow release to Fe(III). The reductase responsible for the transfer of electrons from the capacitor to the soluble carrier has not been identified, but data presented here argue against the involvement of c-type cytochromes.

Silver release from silver nanoparticles in natural waters.

Silver nanoparticles (AgNPs) are used increasingly in consumer products for their antimicrobial properties. This increased use raises ecological concern because of the release of AgNPs into the environment. Once released, zero-valent silver may be oxidized to Ag(+) and the cation liberated or it may persist as AgNPs. The chemical form of Ag has implications for its toxicity; it is therefore crucial to characterize the persistence of AgNPs to predict their ecotoxicological potential. In this study, we evaluated the release of Ag from AgNPs of various sizes exposed to river and lake water for up to 4 months. Several AgNP-capping agents were also considered: polyvinylpyrrolidone (PVP), tannic acid (Tan), and citric acid (Cit). We observed a striking difference between 5, 10, and 50 nm AgNPs, with the latter being more resistant to dissolution in oxic water on a mass basis. However, the difference decreased when Ag was surface-area-normalized, suggesting an important role of the surface area in determining Ag loss. We propose that rapid initial Ag(+) release was attributable to desorption of Ag(+) from nanoparticle surfaces. We also observed that PVP- and Tan-AgNPs are more prone to Ag(+) release than Cit-AgNPs. In addition, it is likely that oxidative dissolution also occurs but at a slower rate. This study clearly shows that small AgNPs (5 nm, PVP and Tan) dissolve rapidly and almost completely, while larger AgNPs (50 nm) have the potential to persist for an extended period of time and could serve as a continuous source of Ag ions.

Role of proteins in controlling selenium nanoparticle size.

This work investigates the potential for harnessing the association of bacterial proteins to biogenic selenium nanoparticles (SeNPs) to control the size distribution and the morphology of the resultant SeNPs. We conducted a proteomic study and compared proteins associated with biogenic SeNPs produced by E. coli to chemically synthesized SeNPs as well as magnetite nanoparticles. We identified four proteins (AdhP, Idh, OmpC, AceA) that bound specifically to SeNPs and observed a narrower size distribution as well as more spherical morphology when the particles were synthesized chemically in the presence of proteins. A more detailed study of AdhP (alcohol dehydrogenase propanol-preferring) confirmed the strong affinity of this protein for the SeNP surface and revealed that this protein controlled the size distribution of the SeNPs and yielded a narrow size distribution with a three-fold decrease in the median size. These results support the assertion that protein may become an important tool in the industrial-scale synthesis of SeNPs of uniform size and properties.