35 resultados para Electron discovery


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Journal of Electroanalytical Chemistry 541 (2003) 153-162

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Dissertation submitted in partial fulfilment of the requirements for the Degree of Master of Science in Geospatial Technologies

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Dissertation submitted in partial fulfilment of the requirements for the Degree of Master of Science in Geospatial Technologies

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The photo-absorption cross section of trifluoromethyl sulphur pentafluoride, SF5CF3 has been measured using synchrotron radiation in the range of 4–11 eV (310 nm > l > 110 nm) and comparison made with electron energy loss spectroscopy (EELS). The measured VUV cross sections are used to derive the photolysis rate of SF5CF3 in the terrestrial atmosphere. It is estimated that the lifetime for this molecule is the order of a 1000 years and the calculated global warming potential (GWP) is found to be between 17000 and 18100, making it one of the most potent global warming gases in the terrestrial atmosphere.

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A novel two-component enzyme system from Escherichia coli involving a flavorubredoxin (FlRd) and its reductase was studied in terms of spectroscopic, redox, and biochemical properties of its constituents. FlRd contains one FMN and one rubredoxin (Rd) center per monomer. To assess the role of the Rd domain, FlRd and a truncated form lacking the Rd domain (FlRd¢Rd), were characterized. FlRd contains 2.9 ( 0.5 iron atoms/subunit, whereas FlRd¢Rd contains 2.1 ( 0.6 iron atoms/subunit. While for FlRd one iron atom corresponds to the Rd center, the other two irons, also present in FlRd¢Rd, are most probably due to a di-iron site. Redox titrations of FlRd using EPR and visible spectroscopies allowed us to determine that the Rd site has a reduction potential of -140 ( 15 mV, whereas the FMN undergoes reduction via a red-semiquinone, at -140 ( 15 mV (Flox/Flsq) and -180 ( 15 mV (Flsq/Flred), at pH 7.6. The Rd site has the lowest potential ever reported for a Rd center, which may be correlated with specific amino acid substitutions close to both cysteine clusters. The gene adjacent to that encoding FlRd was found to code for an FAD-containing protein, (flavo)rubredoxin reductase (FlRd-reductase), which is capable of mediating electron transfer from NADH to DesulfoVibrio gigas Rd as well as to E. coli FlRd. Furthermore, electron donation was found to proceed through the Rd domain of FlRd as the Rd-truncated protein does not react with FlRd-reductase. In vitro, this pathway links NADH oxidation with dioxygen reduction. The possible function of this chain is discussed considering the presence of FlRd homologues in all known genomes of anaerobes and facultative aerobes.

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Thesis presented at the Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, to obtain a Master degree in Conservation and Restoration,Specialization in Textiles

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Dissertation presented to obtain a PhD degree in Biochemistry at the Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa

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A thesis submitted to the University of Innsbruck for the doctor degree in Natural Sciences, Physics and New University of Lisbon for the doctor degree in Physics, Atomic and Molecular Physics

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Dissertation presented to obtain the Ph.D degree in Bioinformatics

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Dissertação para obtenção do Grau de Doutor em Engenharia Física

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Dissertação para obtenção do Grau de Mestre em Engenharia Química e Bioquímica

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Dissertação para obtenção do Grau de Doutor em Engenharia Biomédica

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J Biol Inorg Chem (2011) 16:1241–1254 DOI 10.1007/s00775-011-0812-9

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Biochem. J. (2011) 438,485–494 doi:10.1042/BJ20110836

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J Biol Inorg Chem (2011) 16:881–888 DOI 10.1007/s00775-011-0785-8