Pacific Northwest National Laboratory

About: Pacific Northwest National Laboratory is a facility organization based out in Richland, Washington, United States. It is known for research contribution in the topics: Catalysis & Aerosol. The organization has 11581 authors who have published 27934 publications receiving 1120489 citations. The organization is also known as: PNL & PNNL.

Supercritical fluid synthesis and characterization of catalytic metal nanoparticles on carbon nanotubes

Abstract: A rapid, convenient and environmentally benign method has been developed for the fabrication of metal nanoparticle–multiwall carbon nanotube (MWCNT) composites. Nanoparticles of palladium, rhodium and ruthenium are deposited onto functionalized MWCNTs through a simple hydrogen reduction of metal–β-diketone precursors in supercritical carbon dioxide, and are characterized by transmission electron microscopy (TEM), energy dispersive X-ray spectroscopy (EDS) and X-ray photoelectron spectroscopy (XPS) analyses. These highly dispersed nanoparticles, with a narrow range of size distribution and good adhesion on MWCNT surfaces, are expected to exhibit promising catalytic properties for a variety of chemical reactions. Preliminary experiments demonstrate that Pd nanoparticles supported on MWCNTs are effective catalysts for hydrogenation of olefins in carbon dioxide. The Pd nanoparticle–MWCNT composite also shows a high electrocatalytic activity in oxygen reduction for potential fuel cell application.

Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1.

Abstract: Shewanella oneidensis MR-1 is a facultatively anaerobic bacterium capable of using soluble and insoluble forms of manganese [Mn(III/IV)] and iron [Fe(III)] as terminal electron acceptors during anaerobic respiration. To assess the structural association of two outer membrane-associated c-type decaheme cytochromes (i.e., OmcA [SO1779] and MtrC [SO1778]) and their ability to reduce soluble Fe(III)-nitrilotriacetic acid (NTA), we expressed these proteins with a C-terminal tag in wild-type S. oneidensis and a mutant deficient in these genes (i.e., omcA mtrC). Endogenous MtrC copurified with tagged OmcA in wild-type Shewanella, suggesting a direct association. To further evaluate their possible interaction, both proteins were purified to near homogeneity following the independent expression of OmcA and MtrC in the omcA mtrC mutant. Each purified cytochrome was confirmed to contain 10 hemes and exhibited Fe(III)-NTA reductase activity. To measure binding, MtrC was labeled with the multiuse affinity probe 4,5-bis(1,3,2-dithioarsolan-2-yl)fluorescein (1,2-ethanedithiol)2, which specifically associates with a tetracysteine motif engineered at the C terminus of MtrC. Upon titration with OmcA, there was a marked increase in fluorescence polarization indicating the formation of a high-affinity protein complex (Kd < 500 nM) between MtrC and OmcA whose binding was sensitive to changes in ionic strength. Following association, the OmcA-MtrC complex was observed to have enhanced Fe(III)-NTA reductase specific activity relative to either protein alone, demonstrating that OmcA and MtrC can interact directly with each other to form a stable complex that is consistent with their role in the electron transport pathway of S. oneidensis MR-1.

Clustering Millions of Tandem Mass Spectra

Abstract: Tandem mass spectrometry (MS/MS) experiments often generate redundant data sets containing multiple spectra of the same peptides. Clustering of MS/MS spectra takes advantage of this redundancy by identifying multiple spectra of the same peptide and replacing them with a single representative spectrum. Analyzing only representative spectra results in significant speed-up of MS/MS database searches. We present an efficient clustering approach for analyzing large MS/MS data sets (over 10 million spectra) with a capability to reduce the number of spectra submitted to further analysis by an order of magnitude. The MS/MS database search of clustered spectra results in fewer spurious hits to the database and increases number of peptide identifications as compared to regular nonclustered searches. Our open source software MS-Clustering is available for download at http://peptide.ucsd.edu or can be run online at http://proteomics.bioprojects.org/MassSpec.

Ultra‐Thick, Low‐Tortuosity, and Mesoporous Wood Carbon Anode for High‐Performance Sodium‐Ion Batteries

Abstract: Sodium-ion batteries (SIBs) have attracted extensive interest in the past few years because of the low cost and abundance of sodium resources and hence the potential for grid scale energy storage. Developing low cost electrode materials, particularly anode materials, is the key for further promoting the application of SIBs. Here, we for the first time report a self-standing porous carbon anode directly from natural wood for SIBs, which processes following advantages: (i) ultra-thick carbon anode with a high areal capacity, for example a capacity of 13.6 mAh cm-2 was delivered when the thickness reached 0.85 mm; (ii) low tortuosity, where numerous inherited aligned channels in the wood carbon provide a rapid ion transport path; (iii) porous nature enables a fast ion transfer between the carbon electrode and the electrolyte; (iv) 100% utilization of the wood carbon that conductive additives, binders, and current-collectors are not needed; v) when coupling a Na3V2(PO4)3 cathode with the wood carbon anode, a high capacity of 80 mAh g-1 was obtained at 0.5 C rate (base on cathode) and excellent cycling stability of 300 cycles was also achieved, which demonstrated the promising performance of earth-abundant wood derived carbon material.