39 resultados para TRANSFER EXCITED-STATES


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The most important processes for the creation of S12+ to S14+ ions excited states from the ground configurations of S9+ to S14+ ions in an electron cyclotron resonance ion source, leading to the emission of K X-ray lines, are studied. Theoretical values for inner-shell excitation and ionization cross sections, including double KL and triple KLL ionization, transition probabilities and energies for the deexcitation processes, are calculated in the framework of the multi-configuration Dirac-Fock method. With reasonable assumptions about the electron energy distribution, a theoretical K$\alpha$ X-ray spectrum is obtained, which is compared to recent experimental data.

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

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Dissertação para obtenção do Grau de Doutor em Engenharia Física

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Journal of Electroanalytical Chemistry 541 (2003) 153-162

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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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Paper presented at the 9th European Conference on Knowledge Management, Southampton Solent University, Southampton, UK, 4-5 Sep. 2008. URL: http://academic-conferences.org/eckm/eckm2008/eckm08-home.htm

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FCM: UC Bioquímica I - PhD Thesis

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

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Dissertação apresentada na Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa 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 Doutor em Biologia

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Dissertação para obtenção do Grau de Mestre em Engenharia Electrotécnica e de Computadores

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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