University of Oviedo

About: University of Oviedo is a education organization based out in Oviedo, Spain. It is known for research contribution in the topics: Population & Large Hadron Collider. The organization has 13423 authors who have published 31649 publications receiving 844799 citations. The organization is also known as: Universidá d'Uviéu & Universidad de Oviedo.

A Universal-Input Single-Stag2e High-Power-Factor Power Supply for HB-LEDs Based on Integrated Buck–Flyback Converter

Abstract: Due to the high rise in luminous efficiency that high-brightness light-emitting diodes (HB-LEDs) have experienced in recent years, many new applications have been researched. This paper covers a streetlight LED application using the offline integrated buck-flyback converter (IBFC) developed in previous works. In this application, the converter is used to provide power-factor correction from a universal ac source. A control loop using the LM3524 IC has been implemented for testing the feasibility of Enabling pulsewidth modulation dimming mode. First, the LED load has been linearized and modeled in order to calculate the IBFC topology properly. Second, the converter has been designed and tested at the laboratory. The converter has also been modeled in order to design a fixed-frequency constant-current control. The dynamics of all the stages involved in the closed loop have been taken into account in order to develop an adequate controller. Finally, the experimental results obtained from the laboratory tests are discussed.

Deciphering the biosynthesis pathway of the antitumor thiocoraline from a marine actinomycete and its expression in two Streptomyces species

Abstract: Thiocoraline is a thiodepsipeptide antitumor compound produced by two actinomycetes Micromonospora sp. ACM2-092 and Micromonospora sp. ML1, isolated from two marine invertebrates (a soft coral and a mollusc) found of the Indian Ocean coast of Mozambique. By using oligoprimers derived from nonribosomal peptide synthetase (NRPS) consensus sequences, six PCR fragments containing putative NRPS adenylation domains were amplified from the chromosome of Micromonospora sp. ML1. Insertional inactivation of each adenylation domain showed that two of them generated nonproducing mutants, thereby indicating that these domains were involved in thiocoraline biosynthesis. Sequencing of a 64.6 kbp DNA region revealed the presence of 36 complete open reading frames (ORFs) and two incomplete ones. Heterologous expression of a region of about 53 kbp, containing 26 of the ORFs, in Streptomyces albus and S. lividans led to the production of thiocoraline in these streptomycetes. Surprisingly, the identified gene cluster contains more NRPS modules than expected on the basis of the number of amino acids of thiocoraline. TioR and TioS would most probably constitute the NRPS involved in the biosynthesis of the thiocoraline backbone, according to the colinearity of the respective modules. It is proposed that two other NRPSs, TioY and TioZ, could be responsible for the biosynthesis of a small peptide molecule which could be involved in regulation of the biosynthesis of thicoraline in Micromonospora sp. ML1. In addition, a pathway is proposed for the biosynthesis of the unusual starter unit, 3-hydroxy-quinaldic acid.