1,271 research outputs found
Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties
Nature has evolved several unique biomineralization strategies to direct the synthesis and growth of inorganic materials. These natural systems are complex, involving the interaction of multiple biomolecules to catalyze biomineralization and template growth. Herein we describe the first report to our knowledge of a single enzyme capable of both catalyzing mineralization in otherwise unreactive solution and of templating nanocrystal growth. A recombinant putative cystathionine γ-lyase (smCSE) mineralizes CdS from an aqueous cadmium acetate solution via reactive H2S generation from l-cysteine and controls nanocrystal growth within the quantum confined size range. The role of enzymatic nanocrystal templating is demonstrated by substituting reactive Na2S as the sulfur source. Whereas bulk CdS is formed in the absence of the enzyme or other capping agents, nanocrystal formation is observed when smCSE is present to control the growth. This dual-function, single-enzyme, aerobic, and aqueous route to functional material synthesis demonstrates the powerful potential of engineered functional material biomineralization
Single enzyme direct biomineralization of ZnS, ZnxCd1�xS and ZnxCd1�xS–ZnS quantum confined nanocrystals
ZnS, ZnxCd1−xS, and ZnxCd1−xS–ZnS quantum dots were synthesized in the aqueous phase at room temperature via biomineralization enabled by a single enzyme in solution.</p
Single enzyme direct biomineralization of CdSe and CdSe-CdS core-shell quantum dots
Biomineralization is the process by which biological systems synthesize inorganic materials. Herein, we demonstrate an engineered cystathionine γ-lyase enzyme, smCSE that is active for the direct aqueous phase biomineralization of CdSe and CdSe-CdS core-shell nanocrystals. The nanocrystals are formed in an otherwise unreactive buffered solution of Cd acetate and selenocystine through enzymatic turnover of the selenocystine to form a reactive precursor, likely H2Se. The particle size of the CdSe core nanocrystals can be tuned by varying the incubation time to generated particle sizes between 2.74 ± 0.63 nm and 4.78 ± 1.16 nm formed after 20 min and 24 h of incubation, respectively. Subsequent purification and introduction of l-cysteine as a sulfur source facilitates the biomineralization of a CdS shell onto the CdSe cores. The quantum yield of the resulting CdSe-CdS core-shell particles is up to 12% in the aqueous phase; comparable to that reported for more traditional chemical synthesis routes for core-shell particles of similar size with similar shell coverage. This single-enzyme route to functional nanocrystals synthesis reveals the powerful potential of biomineralization processes
Biomineralized CdS quantum dot nanocrystals: optimizing synthesis conditions and improving functional properties by surface modification
An engineered strain of Stenotrophomonas maltophilia (SMCD1) is capable of the direct extracellular biomineralization of CdS quantum dot nanocrystals from buffered aqueous solution of cadmium acetate and l-cysteine without the addition of a chemically reactive precursor. Nanocrystal synthesis is strongly influenced by both the l-cysteine/cadmium acetate ratio and pH of the solution. The observed trends are consistent with l-cysteine acting as both a sulfur source and nanocrystal capping agent. Enzymatic turnover of l-cysteine by a putative cystathionine γ-lyase forms reactive sulfur in solution, removing the requirement for addition of reactive sodium sulfide typical of most other biomineralization approaches. The utility of the biomineralized quantum dots is demonstrated by phase transfer from the aqueous to the organic phase and subsequent incorporation into a quantum dot sensitized solar cell and chemical growth of a ZnS shell onto the biomineralized CdS core
Biomineralization of PbS and PbS-CdS core-shell nanocrystals and their application in quantum dot sensitized solar cells
Biomineralization utilizes biological systems to synthesize functional inorganic materials for application in diverse fields. In the current work, we enable biomineralization of quantum confined PbS and PbS–CdS core–shell nanocrystals and demonstrate their application in quantum dot sensitized solar cells (QDSSCs). An engineered strain of Stenotrophomonas maltophilia is utilized to generate a cystathionine γ-lyase that is active for the biomineralization of metal sulfide nanocrystals from a buffered aqueous solution of metal salts and L-cysteine. In the presence of lead acetate, this enzymatic route generates rock salt structured PbS nanocrystals. Controlling the growth conditions yields ∼4 nm PbS crystals with absorption and photoluminescence peaks at 910 nm and 1080 nm, respectively, consistent with the expected strong quantum confinement of PbS at this size. Quantum yields (QY) of the biomineralized PbS quantum dots, determined after phase transfer to the organic phase, range between 16 and 45%. These are the highest reported QY values for any biomineralized quantum dot materials to date and are comparable with QYs reported for chemically synthesized materials. Subsequent exposure to cadmium acetate results in the biomineralization of a thin CdS shell on the PbS core with a resultant blue-shift in optical properties. The photoluminescence peak shifts to 980 nm, consistent with the expected decrease in band gap energy of a PbS–CdS core–shell heterostructured quantum dot. HAADF-STEM imaging confirms the crystalline structure and size of the particles with complimentary XEDS analysis confirming the presence of Cd, Pb, and S in individual nanocrystals. Integration of these QDs into QDSSCs yields open circuit potentials of 0.43 V and 0.59 V for PbS and PbS–CdS, respectively, consistent with expectations for these materials and previously reported values for chemically synthesized QDs
Enzymatic biomineralization of biocompatible CuInS2, (CuInZn)S2 and CuInS2/ZnS core/shell nanocrystals for bioimaging
This work demonstrates a bioenabled, aqueous phase, room temperature route to synthesize CuInS2/ZnS quantum dots conjugated to IgG antibodies for fluorescent tagging of THP-1 leukemia cells.</p
STITCHER: Dynamic assembly of likely amyloid and prion β-structures from secondary structure predictions
The supersecondary structure of amyloids and prions, proteins of intense clinical and biological interest, are difficult to determine by standard experimental or computational means. In addition, significant conformational heterogeneity is known or suspected to exist in many amyloid fibrils. Previous work has demonstrated that probability-based prediction of discrete β-strand pairs can offer insight into these structures. Here, we devise a system of energetic rules that can be used to dynamically assemble these discrete β-strand pairs into complete amyloid β-structures. The STITCHER algorithm progressively ‘stitches’ strand-pairs into full β-sheets based on a novel free-energy model, incorporating experimentally observed amino-acid side-chain stacking contributions, entropic estimates, and steric restrictions for amyloidal parallel β-sheet construction. A dynamic program computes the top 50 structures and returns both the highest scoring structure and a consensus structure taken by polling this list for common discrete elements. Putative structural heterogeneity can be inferred from sequence regions that compose poorly. Predictions show agreement with experimental models of Alzheimer's amyloid beta peptide and the Podospora anserina Het-s prion. Predictions of the HET-s homolog HET-S also reflect experimental observations of poor amyloid formation. We put forward predicted structures for the yeast prion Sup35, suggesting N-terminal structural stability enabled by tyrosine ladders, and C-terminal heterogeneity. Predictions for the Rnq1 prion and alpha-synuclein are also given, identifying a similar mix of homogenous and heterogeneous secondary structure elements. STITCHER provides novel insight into the energetic basis of amyloid structure, provides accurate structure predictions, and can help guide future experimental studies. Proteins 2011
Direct single-enzyme biomineralization of catalytically active ceria and ceria-zirconia nanocrystals
Biomineralization is an intriguing approach to the synthesis of functional inorganic materials for energy applications whereby biological systems are engineered to mineralize inorganic materials and control their structure over multiple length scales under mild reaction conditions. Herein we demonstrate a single-enzyme-mediated biomineralization route to synthesize crystalline, catalytically active, quantum-confined ceria (CeO2–x) and ceria–zirconia (Ce1–yZryO2–x) nanocrystals for application as environmental catalysts. In contrast to typical anthropogenic synthesis routes, the crystalline oxide nanoparticles are formed at room temperature from an otherwise inert aqueous solution without the addition of a precipitant or additional reactant. An engineered form of silicatein, rCeSi, as a single enzyme not only catalyzes the direct biomineralization of the nanocrystalline oxides but also serves as a templating agent to control their morphological structure. The biomineralized nanocrystals of less than 3 nm in diameter are catalytically active toward carbon monoxide oxidation following an oxidative annealing step to remove carbonaceous residue. The introduction of zirconia into the nanocrystals leads to an increase in Ce(III) concentration, associated catalytic activity, and the thermal stability of the nanocrystals
QCD
We discuss issues of QCD at the LHC including parton distributions, Monte
Carlo event generators, the available next-to-leading order calculations,
resummation, photon production, small x physics, double parton scattering, and
backgrounds to Higgs production.Comment: 115 pages, Latex, 47 figures, to appear in the Report of the ``1999
CERN Workshop on SM Physics (and more) at the LHC'', S. Catani, M. Dittmar,
D. Soper, W.J. Stirling, S. Tapprogge (convenors
Control of electron transport routes through redox-regulated redistribution of respiratory complexes
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