Alexandre, J, Feio G, Marvao MR, Figueiredo J.
2004.
Correlation between high power proton T(2) NMR relaxation and macroscopic viscoelastic properties. Advanced Materials Forum Ii. 455-456(
R. Martins, E. Fortunato, Ferreira, I., Dias, C., Eds.).:459-462.
Abstractn/a
Moniz, A.
2004.
Elementos para o estudo de um caso de sucesso na montagem automóvel em Portugal: a Opel Portugal[Elements for the study of a success case in automobile assembly: the Opel Portugal]. , Number 5938: University Library of Munich, Germany
AbstractThe interest to study this factory of GM group in Portugal is due to the facto of being one of the oldest assembly lines of the automotive sector still operating in Portugal (it was founded in 1963). Besides that, it went recently across a very intensive technological change, and then would be interesting to know the organisation of work model chose. The Opel factory occupies at the moment the former one that belonged to Ford Lusitana. There it has being under production some modules that feed the assembly line on JIT and in sequence. Although there were severe difficulties to implement the case study at Opel, this report could be done using secondary information and several interviews at the factory and initial visits. This Opel factory was recently closed down in the frame of a GM European strategy for re-structuring.
Valente, AA, Petrovski Z, Branco LC, Afonso CAM, Pillinger M, Lopes AD, Romao CC, Nunes CD, Goncalves IS.
2004.
Epoxidation of cyclooctene catalyzed by dioxomolybdenum(VI) complexes in ionic liquids. Journal of Molecular Catalysis a-Chemical. 218:5-11., Number 1
Abstractn/a
Carvalho, AL, Goyal A, Prates JAM, Bolam DN, Gilbert HJ, Pires VMR, Ferreira LMA, Planas A, Romao MJ, Fontes C.
2004.
The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site. Journal of Biological Chemistry. 279:34785-34793., Number 33
Abstractn/a
Ortigueira, MD, Coito F.
2004.
From Differences to Derivatives. Fractional Calculus and Applied Analysis. 7:459., Number 4: INSTITUTE OF MATHEMATICS AND INFORMATICS BULGARIAN ACADEMY OF SCIENCES
Abstract
Faustino, P, Miranda A, Silva MD, Alves C, Pinanco I, Ferreira C, Seixas MT, Pina F, Romao L.
2004.
Hb Yaounde beta 134(H12)Val -> Ala in association with Hb C beta 6(A3)Glu -> Lys in a Caucasian Portuguese family. Hemoglobin. 28:229-235., Number 3
Abstractn/a
Moncada, MC, Fernandez D, Lima JC, Parola AJ, Lodeiro C, Folgosa F, Melo MJ, Pina F.
2004.
Multistate properties of 7-(N,N-diethylamino)-4 '-hydroxyflavylium. An example of an unidirectional reaction cycle driven by pH. Organic & Biomolecular Chemistry. 2:2802-2808., Number 19
Abstractn/a
Pauleta, SR, Guerlesquin F, Goodhew CF, Devreese B, Van Beeumen J, Pereira AS, Moura I, Pettigrew GW.
2004.
Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase. Biochemistry. {43}:{11214-11225}., Number {35}, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA: AMER CHEMICAL SOC
AbstractThe gene for pseudoazurin was isolated from Paracoccus pantotrophus LMD 52.44 and expressed in a heterologous system with a yield of 54.3 mg of pure protein per liter of culture. The gene and protein were shown to be identical to those from P. pantotrophus LMD 82.5. The extinction coefficient of the protein was re-evaluated and was found to be 3.00 mM(-1) cm(-1) at 590 nm. It was confirmed that the oxidized protein is in a weak monomer/dimer equilibrium that is ionic- strength-dependent. The pseudoazurin was shown to be a highly active electron donor to cytochrome c peroxidase, and activity showed an ionic strength dependence consistent with an electrostatic interaction. The pseudoazurin has a very large dipole moment, the vector of which is positioned at the putative electron-transfer site, His81, and is conserved in this position across a wide range of blue copper proteins. Binding of the peroxidase to pseudoazurin causes perturbation of a set of NMR resonances associated with residues on the His81 face, including a ring of lysine residues. These lysines are associated with acidic residues just back from the rim, the resonances of which are also affected by binding to the peroxidase. We propose that these acidic residues moderate the electrostatic influence of the lysines and so ensure that specific charge interactions do not form across the interface with the peroxidase.
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