École Polytechnique Fédérale de Lausanne

About: École Polytechnique Fédérale de Lausanne is a facility organization based out in Lausanne, Switzerland. It is known for research contribution in the topics: Population & Catalysis. The organization has 44041 authors who have published 98296 publications receiving 4372092 citations. The organization is also known as: EPFL & ETHL.

Generation of intense, carrier-envelope phase-locked few-cycle laser pulses through filamentation

Abstract: Intense, well-controlled light pulses with only a few optical cycles start to play a crucial role in many fields of physics, such as attosecond science. We present an extremely simple and robust technique to generate such carrier-envelope offset (CEO) phase locked few-cycle pulses, relying on self-guiding of intense 43-fs, 0.84 mJ optical pulses during propagation in a transparent noble gas. We have demonstrated 5.7-fs, 0.38 mJ pulses with an excellent spatial beam profile and discuss the potential for much shorter pulses. Numerical simulations confirm that filamentation is the mechanism responsible for pulse shortening. The method is widely applicable and much less sensitive to experimental conditions such as beam alignment, input pulse duration or gas pressure as compared to gas-filled hollow fibers.

A cobalt complex redox shuttle for dye-sensitized solar cells with high open-circuit potentials

Abstract: Dye-sensitized solar cells are a promising alternative to traditional inorganic semiconductor-based solar cells. Here we report an open-circuit voltage of over 1,000 mV in mesoscopic dye-sensitized solar cells incorporating a molecularly engineered cobalt complex as redox mediator. Cobalt complexes have negligible absorption in the visible region of the solar spectrum, and their redox properties can be tuned in a controlled fashion by selecting suitable donor/acceptor substituents on the ligand. This approach offers an attractive alternate to the traditional I(3)(-)/I(-) redox shuttle used in dye-sensitized solar cells. A cobalt complex using tridendate ligands [Co(bpy-pz)(2)](3+/2+)(PF(6))(3/2) as redox mediator in combination with a cyclopentadithiophene-bridged donor-acceptor dye (Y123), adsorbed on TiO(2), yielded a power conversion efficiency of over 10% at 100 mW cm(-2). This result indicates that the molecularly engineered cobalt redox shuttle is a legitimate alternative to the commonly used I(3)(-)/I(-) redox shuttle.

Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa

Abstract: The opportunistic human pathogen Pseudomonas aeruginosa produces a variety of virulence factors, including exotoxin A, elastase, alkaline protease, alginate, phospholipases, and extracellular rhamnolipids. The previously characterized rhlABR gene cluster encodes a regulatory protein (RhlR) and a rhamnosyltransferase (RhlAB), both of which are required for rhamnolipid synthesis. Another gene, rhII, has now been identified downstream of the rhlABR gene cluster. The putative RhlI protein shares significant sequence similarity with bacterial autoinducer synthetases of the LuxI type. A P. aeruginosa rhlI mutant strain carrying a disrupted rhlI gene was unable to produce rhamnolipids and lacked rhamnosyltransferase activity. Rhamnolipid synthesis was restored by introducing a wild-type rhlI gene into such strains or, alternatively, by adding either the cell-free spent supernatant from a P. aeruginosa wild-type strain or synthetic N-acylhomoserine lactones. Half-maximal induction of rhamnolipid synthesis in the rhlI mutant strain required 0.5 microM N-butyrylhomoserine lactone or 10 microM N-(3-oxohexanoyl)homoserine lactone. The P. aeruginosa rhlA promoter was active in the heterologous host Pseudomonas putida when both the rhlR and rhlI genes were present or when the rhlR gene alone was supplied together with synthetic N-acylhomoserine lactones. The RhlR-RhlI regulatory system was found to be essential for the production of elastase as well, and cross-communication between the RhlR-RhlI rhamnolipid regulatory system and the LasR-LasI elastase regulatory system was demonstrated.