Antecedentes Medievais da Ruptura com Roma

Miguel Alarcão, “Antecedentes Medievais da Ruptura com Roma.” Via Panorâmica: Revista Electrónica de Estudos Anglo- Americanos /An Anglo-American Studies Journal 2.ª ser. 1 (2008): 142- 155. Web. http:// ler.letras.up.pt>.

Spectroscopic Studies and Characterization of a Novel Electron-Transfer Chain

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.

Kinetic, Structural, and EPR Studies Reveal That Aldehyde Oxidoreductase from Desulfovibrio gigas Does Not Need a Sulfido Ligand for Catalysis and Give Evidence for a Direct Mo-C Interaction in a Biological System

J. Am. Chem. Soc., 2009, 131 (23), pp 7990–7998 DOI: 10.1021/ja809448r

Electron transfer complex between nitrous oxide reductase and cytochrome c552 from Pseudomonas nautica: kinetic, nuclear magnetic resonance, and docking studies

Biochemistry. 2008 Oct 14;47(41):10852-62. doi: 10.1021/bi801375q

Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria

Acc. Chem. Res., 2006, 39 (10), pp 788–796 DOI: 10.1021/ar050104k

Attractiveness of European masters under Bologna constraints: The South American case

This paper studies strategies to attract students from outside Europe to European preexperience masters. We characterize the value added by such masters through interviews with key players at the universities and multinational recruiting corporations. We considered a strategy for segmenting international students in the US and extended it to the European market. We have analyzed data from international applications to Nova SBE as a proxy for applications in European institutions. Based on that analysis we conclude with recommendations to attract suitable candidates from outside Europe. In particular we also provided three different solutions to attract students from the southern hemisphere: we conclude that European institutions should (a) increase the spring semester intake, (b) provide bridging courses for some students, or (c) could place some accepted candidates in internships before starting classes.