35 resultados para Binuclear Metal Center


Relevância:

80.00% 80.00%

Publicador:

Resumo:

Protein Science (2002), 11:2464–2470

Relevância:

80.00% 80.00%

Publicador:

Resumo:

Inorganic Chemistry 50(21):10600-7

Relevância:

30.00% 30.00%

Publicador:

Resumo:

Biochemistry, 2011, 50 (20), pp 4251–4262 DOI: 10.1021/bi101605p

Relevância:

20.00% 20.00%

Publicador:

Resumo:

The aim of the TeleRisk Project on labour relations and professional risks within the context of teleworking in Portugal – supported by IDICT – Institute for Development and Inspection of Working Conditions (Ministry of Labour), is to study the practices and forms of teleworking in the manufacturing sectors in Portugal. The project chose also the software industry as a reference sector, even though it does not intend to exclude from the study any other sector of activity or the so-called “hybrid” forms of work. However, the latter must have some of the characteristics of telework. The project thus takes into account the so-called “traditional” sectors of activity, namely textile and machinery and metal engineering (machinery and equipment), not usually associated to this type of work. However, telework could include, in the so-called “traditional” sectors, other variations that are not found in technologically based sectors. One of the evaluation methods for the dynamics associated to telework consisted in carrying out surveys by means of questionnaires, aimed at employers in the sectors analysed. This paper presents some of the results of those surveys. It is important to mention that, being a preliminary analysis, it means that it does not pretend to have exhausted all the issues in the survey, but has meant that it shows the bigger tendencies, in terms of teleworking practices, of the Portuguese industry.

Relevância:

20.00% 20.00%

Publicador:

Resumo:

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

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Dissertation submitted for obtainment of the Master’s Degree in Biotechnology, by the Universidade Nova de Lisboa, Faculdade de Ciências e Tecnologia

Relevância:

20.00% 20.00%

Publicador:

Resumo:

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

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Febs Journal (2009)276:1776-1786

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Dissertação apresentada na Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa para obtenção do grau de Mestre em Biotecnologia

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Dissertação apresentada para cumprimento dos requisitos necessários à obtenção do grau de Mestre em Estudos sobre as Mulheres

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Disserta ção apresentada para obten ção do Grau de Mestre em Engenharia Química e Bioquímica

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Ligand K-edge XAS of an [Fe3S4]0 model complex is reported. The pre-edge can be resolved into contributions from the í2Ssulfide, í3Ssulfide, and Sthiolate ligands. The average ligand-metal bond covalencies obtained from these pre-edges are further distributed between Fe3+ and Fe2.5+ components using DFT calculations. The bridging ligand covalency in the [Fe2S2]+ subsite of the [Fe3S4]0 cluster is found to be significantly lower than its value in a reduced [Fe2S2] cluster (38% vs 61%, respectively). This lowered bridging ligand covalency reduces the superexchange coupling parameter J relative to its value in a reduced [Fe2S2]+ site (-146 cm-1 vs -360 cm-1, respectively). This decrease in J, along with estimates of the double exchange parameter B and vibronic coupling parameter ì2/k-, leads to an S ) 2 delocalized ground state in the [Fe3S4]0 cluster. The S K-edge XAS of the protein ferredoxin II (Fd II) from the D. gigas active site shows a decrease in covalency compared to the model complex, in the same oxidation state, which correlates with the number of H-bonding interactions to specific sulfur ligands present in the active site. The changes in ligand-metal bond covalencies upon redox compared with DFT calculations indicate that the redox reaction involves a two-electron change (one-electron ionization plus a spin change of a second electron) with significant electronic relaxation. The presence of the redox inactive Fe3+ center is found to decrease the barrier of the redox process in the [Fe3S4] cluster due to its strong antiferromagnetic coupling with the redox active Fe2S2 subsite.

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Dissertação para obtenção do Grau de Mestre em Engenharia Química e Bioquímica

Relevância:

20.00% 20.00%

Publicador:

Resumo:

Dissertation presented to obtain the PhD degree in Biochemistry

Relevância:

20.00% 20.00%

Publicador:

Resumo:

J Biol Inorg Chem (2011) 16:1255–1268 DOI 10.1007/s00775-011-0813-8