36 resultados para Electron Diffusion


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Journal of Electroanalytical Chemistry 541 (2003) 153-162

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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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Les rapports complexes entre les différentes façons de faire circuler les idées et les informations ne datent pas de nos jours. A toutes les époques, les messages qui circulent emploient toutes sortes de véhicules et de langages, très souvent complémentaires. Ces véhicules et ces langages n'ont peut-être rien d'extraordinaire. Ils appartiennent au monde des gestes de tous les jours, des gestes qui se répètent et dont la répétition est elle-même importante pour la construction du sens de chaque message. Ces gestes qui sont répétés, qui sont attendus et qui sont reconnus incluent des sons, des images, des comportements, des mots, ou des citations. Il y a donc un rapport qui s'y établit entre répétition et nouveauté, rapport dans lequel la répétition fournit chaque fois une nouvelle information, même si elle est déjà attendue, tandis que leur absence peut représenter l'anxiété, ou même le scandale.

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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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Dissertação para obtenção do Grau de Mestre em Biotecnologia

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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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Dissertação para obtenção do Grau de Doutor em Conservação e Restauro, especialidade Ciências da Conservação

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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