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1994
Pereira, Z, Moniz A, Kovács I.  1994.  {Quality and work organisation in Portuguese industry}, Sep. , Number 7412: University Library of Munich, Germany Abstract

The present communication analyses the relationships between work organisation and quality systems. The analysis is based on results from a study funded by the "Specific Programme for the Development of Portuguese Industry" (PEDIP). The main issues which have been currently associated with work organisation and quality control in the Portuguese industry are characterized. Critical features related to the implementation of quality systems and new methods of work organisation for industrial development are also discussed. A few recommendations are given in order to promote appropriate methods of work organisation for quality improvement within Portuguese industry.

Pereira, Z, Kovács I, Moniz A.  1994.  Quality and work organization with advanced automation in Portugal, Jul. , Number 7567: University Library of Munich, Germany Abstract

In this paper it is analysed the relationships between work organisation and quality systems in firms that uses some forms of advanced automation. Are characterised the existing quality control structures in the Portuguese industry, and the main factors that hidden or fosters the development of sociotechnical methods of quality control organisation strategies. Are analysed some industrial cases that explains more clearly the critical issues of the implementation of quality systems and work organisation systems. A few recommendations are given about the possibilities for the development of new forms of work organisation and the quality systems associated to automated manufacturing systems.

Kovács, I, Moniz A.  1994.  Trends for the development of anthropocentric production systems in small less industrialised countries: The case of Portugal, Jul. , Number 6551: University Library of Munich, Germany Abstract

This paper analyses the problems and trends of the introduction of anthropocentric production systems (APS) in small less industrialized member states of the European Union, specifically the case of Portugal, based on the report for the FAST-Anthropocentric Technology Assessment Project (Monitor Programme) on “Prospects and conditions for APS in Europe by the 21st century”. Research teams from all countries of the European Community, as well as researchers from USA, Japan and Australia were participating in this project. The aim of this paper is to characterize APS and to present some special considerations related to the socioeconomic factors affecting the prospects and conditions for APS in Portugal. APS is defined as a system based on the utilization of skilled human resources and flexible technology adapted to the needs of flexible and participative organization. Among socioeconomic factors, some critical aspects for the development of APS will be focused, namely technological infrastructure, management strategies, perceived impact of introduction of automated systems on the division of labor and organizational structure, educational and vocational training and social actors strategies towards industrial automation. This analysis is based on a sample of industrial firms, built up for qualitative analysis, and on case studies analysis that can be reference examples for further development of APS, and not just for economic policy purposes alone. We have also analyzed the type of existing industrial relations, the union and employer strategies and some aspects of public policies towards the introduction of new technologies in the order to understand the extent to which there exist obstacles to and favorable conditions for the diffusion of anthropocentric systems. Finally some recommendations are presented to stress the trends for the implementation and development of anthropocentric production systems in Portugal.

Pereira, Z, Kovács I, Moniz A.  1994.  {Quality and work organization with advanced automation in Portugal}, Jul. , Number 7567: University Library of Munich, Germany Abstract

In this paper it is analysed the relationships between work organisation and quality systems in firms that uses some forms of advanced automation. Are characterised the existing quality control structures in the Portuguese industry, and the main factors that hidden or fosters the development of sociotechnical methods of quality control organisation strategies. Are analysed some industrial cases that explains more clearly the critical issues of the implementation of quality systems and work organisation systems. A few recommendations are given about the possibilities for the development of new forms of work organisation and the quality systems associated to automated manufacturing systems.

Kovács, I, Moniz A.  1994.  {Trends for the development of anthropocentric production systems in small less industrialised countries: The case of Portugal}, Jul. , Number 6551: University Library of Munich, Germany Abstract

This paper analyses the problems and trends of the introduction of anthropocentric production systems (APS) in small less industrialized member states of the European Union, specifically the case of Portugal, based on the report for the FAST-Anthropocentric Technology Assessment Project (Monitor Programme) on “Prospects and conditions for APS in Europe by the 21st century”. Research teams from all countries of the European Community, as well as researchers from USA, Japan and Australia were participating in this project. The aim of this paper is to characterize APS and to present some special considerations related to the socioeconomic factors affecting the prospects and conditions for APS in Portugal. APS is defined as a system based on the utilization of skilled human resources and flexible technology adapted to the needs of flexible and participative organization. Among socioeconomic factors, some critical aspects for the development of APS will be focused, namely technological infrastructure, management strategies, perceived impact of introduction of automated systems on the division of labor and organizational structure, educational and vocational training and social actors strategies towards industrial automation. This analysis is based on a sample of industrial firms, built up for qualitative analysis, and on case studies analysis that can be reference examples for further development of APS, and not just for economic policy purposes alone. We have also analyzed the type of existing industrial relations, the union and employer strategies and some aspects of public policies towards the introduction of new technologies in the order to understand the extent to which there exist obstacles to and favorable conditions for the diffusion of anthropocentric systems. Finally some recommendations are presented to stress the trends for the implementation and development of anthropocentric production systems in Portugal.

1992
Melo, MJ, Pina F, Macanita AL, Melo EC, Herrmann C, Forster R, Koch H, Wamhoff H.  1992.  PHOTOCHEMISTRY OF 2-(2-FURYL)-BENZIMIDAZOLE (FUBERIDAZOLE). Zeitschrift Fur Naturforschung Section B-a Journal of Chemical Sciences. 47:1431-1437., Number 10 AbstractWebsite
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1990
Fauque, G, Lino AR, Czechowski M, Kang L, Dervartanian DV, Moura JJ, Legall J, Moura I.  1990.  Purification and characterization of bisulfite reductase (desulfofuscidin) from Desulfovibrio thermophilus and its complexes with exogenous ligands, Aug 1. Biochim Biophys Acta. 1040:112-8., Number 1 AbstractWebsite

A dissimilatory bisulfite reductase has been purified from a thermophilic sulfate-reducing bacterium Desulfovibrio thermophilus (DSM 1276) and studied by EPR and optical spectroscopic techniques. The visible spectrum of the purified bisulfite reductase exhibits absorption maxima at 578.5, 392.5 and 281 nm with a weak band around 700 nm. Photoreduction of the native enzyme causes a decrease in absorption at 578.5 nm and a concomitant increase in absorption at 607 nm. When reduced, the enzyme reacts with cyanide, sulfite, sulfide and carbon monoxide to give stable complexes. The EPR spectrum of the native D. thermophilus bisulfite reductase shows the presence of a high-spin ferric signal with g values at 7.26, 4.78 and 1.92. Upon photoreduction the high-spin ferric heme signal disappeared and a typical 'g = 1.94' signal of [4Fe-4S] type cluster appeared. Chemical analyses show that the enzyme contains four sirohemes and eight [4Fe-4S] centers per mol of protein. The molecular mass determined by gel filtration was found to be 175 kDa. On SDS-gel electrophoresis the enzyme presents a main band of 44 to 48 kDa. These results suggest that the bisulfite reductase contains probably one siroheme and two [4Fe-4S] centers per monomer. The dissimilatory bisulfite reductase from D. thermophilus presents some homologous properties with desulfofuscidin, the bisulfite reductase isolated from Thermodesulfobacterium commune (Hatchikian, E.C. and Zeikus, J.G. (1983) J. Bacteriol. 153, 1211-1220).

1988
Kowal, AT, Zambrano IC, Moura I, Moura JJG, Legall J, Johnson MK.  1988.  Electronic and magnetic properties of nickel-substituted rubredoxin: a variable-temperature magnetic circular dichroism study, 1988/04/01. Inorganic Chemistry. 27:1162-1166., Number 7: American Chemical Society AbstractWebsite
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Kremer, DR, Veenhuis M, Fauque G, Peck HD, Legall J, Lampreia J, Moura JJG, Hansen TA.  1988.  Immunocytochemical localization of APS reductase and bisulfite reductase in three <i>Desulfovibrio</i> species. Archives of Microbiology. 150:296-301., Number 3: Springer Berlin / Heidelberg AbstractWebsite

The localization of APS reductase and bisulfite reductase in Desulfovibrio gigas, D. vulgaris Hildenborough and D. thermophilus was studied by immunoelectron microscopy. Polyclonal antibodies were raised against the purified enzymes from each strain. Cells fixed with formaldehyde/glutaraldehyde were embedded and ultrathin sections were incubated with antibodies and subsequently labeled with protein A-gold. The bisulfite reductase in all three strains and APS reductase in d. gigas and D. vulgaris were found in the cytoplasm. The labeling of d. thermophilus with APS reductase antibodies resulted in a distribution of gold particles over the cytoplasmic membrane region. The localization of the two enzymes is discussed with respect to the mechanism and energetics of dissimilatory sulfate reduction.

1987
Werth, MT, Kurtz DM, Moura I, Legall J.  1987.  Proton NMR spectra of rubredoxins: new resonances assignable to .alpha.-CH and .beta.-CH2 hydrogens of cysteinate ligands to iron(II), 1987/01/01. Journal of the American Chemical Society. 109:273-275., Number 1: American Chemical Society AbstractWebsite
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1983
Huynh, BH, Legall J, Dervartanian DV, Peck Jr HD, Krüger HJ, Moura I, Moura JJG, Xavier AV.  1983.  Mössbauer and EPR evidence for nickel and 3Fe cluster in the hydrogenases of D. desulfuricans and D. gigas. Inorganica Chimica Acta. 79:136. AbstractWebsite
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1982
Moura, JJ, Moura I, Huynh BH, Kruger HJ, Teixeira M, DuVarney RC, Dervartanian DV, Xavier AV, Peck, H. D. J, Legall J.  1982.  Unambiguous identification of the nickel EPR signal in 61Ni-enriched Desulfovibrio gigas hydrogenase, Oct 29. Biochem Biophys Res Commun. 108:1388-93., Number 4 AbstractWebsite
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Moura, JJ, Moura I, Kent TA, Lipscomb JD, Huynh BH, Legall J, Xavier AV, Munck E.  1982.  Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mossbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II, Jun 10. J Biol Chem. 257:6259-67., Number 11 AbstractWebsite
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Kruger, HJ, Huynh BH, Ljungdahl PO, Xavier AV, Dervartanian DV, Moura I, Peck, H. D. J, Teixeira M, Moura JJ, Legall J.  1982.  Evidence for nickel and a three-iron center in the hydrogenase of Desulfovibrio desulfuricans, Dec 25. J Biol Chem. 257:14620-3., Number 24 AbstractWebsite

Hydrogenase from Desulfovibrio desulfuricans (ATCC No. 27774) grown in unenriched and in enriched 61Ni and 57Fe media has been purified to apparent homogeneity. Two fractions of enzymes with hydrogenase activity were separated and were termed hydrogenase I and hydrogenase II. they were shown to have similar molecular weights (77,600 for hydrogenase I and 75,500 for hydrogenase II), to be composed of two polypeptide chains, and to contain Ni and non-heme iron. Because of its higher specific activity (152 versus 97) hydrogenase II was selected for EPR and Mossbauer studies. As isolated, hydrogenase II exhibits an "isotropic" EPR signal at g = 2.02 and a rhombic EPR signal at g = 2.3, 2.2, and 2.0. Isotopic substitution of 61Ni proves that the rhombic signal is due to Ni. Combining the Mossbauer and EPR data, the isotropic g = 2.02 EPR signal was shown to originate from a 3Fe cluster which may have oxygenous or nitrogenous ligands. In addition, the Mossbauer data also revealed two [4Fe-4S]2+ clusters iun each molecule of hydrogenase II. The EPR and Mossbauer data of hydrogenase I were found to be identical to those of hydrogenase II, indicating that both enzymes have common metallic centers.

Kent, TA, Moura I, Moura JJG, Lipscomb JD, Huynh BH, Legall J, Xavier AV, Münck E.  1982.  Conversion of [3 Fe-3 S] into [4 Fe-4 S] clusters in a Desulfovibrio gigas ferredoxin and isotopic labeling of iron—sulfur cluster subsites. Febs Letters. 138:55-58., Number 1 AbstractWebsite
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1980
Huynh, BH, Moura JJ, Moura I, Kent TA, Legall J, Xavier AV, Munck E.  1980.  Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mossbauer and EPR studies, Apr 25. J Biol Chem. 255:3242-4., Number 8 AbstractWebsite

The tetrameric form of a Desulfovibrio gigas ferredoxin, named Fd II, mediates electron transfer between cytochrome c3 and sulfite reductase. We have studied two stable oxidation states of this protein with Mossbauer spectroscopy and electron paramagnetic resonance. We found 3 iron atoms/monomer and a spin concentration of 0.9 spins/monomer for the oxidized protein. Taken together, the EPR and Mossbauer data demonstrate conclusively the presence of a spin-coupled structure containing 3 iron atoms and labile sulfur. The Mossbauer data show also that this metal center is structurally similar, if not identical, with the low potential center of a ferredoxin from Azotobacter vinelandii, a novel cluster described recently (Emptage, M.H., Kent, T.A., Huynh, B.H., Rawlings, J., Orme-Johnson, W.H., and Munck, E. (1980) J. Biol. Chem. 255, 1793-1796).

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