Pina, João, Pedro Pereira, S. Valtchev, A. Gonçalves, Mário Neves, and A. Rodrigues. "
A test rig for thrust force measurements f an all HTS linear synchronous motor."
8th European Conference on Applied Superconductivity (EUCAS). 2007.
AbstractThis paper presents the design of a test rig for an all HTS linear synchronous motor. Although this motor showed to have several unattractive characteristics, its design raised a number of problems which must be considered in future HTS machines design. HTS electromagnetic properties led to the development of new paradigms in electrical machines and power systems, as e. g. in some cases iron removal and consequent assembly of lighter devices. This is due to superconductor's ability to carry high currents with minimum losses and consequent generation in the surrounding air of flux densities much higher than the allowed by ferromagnetic saturation. However, severe restrictions in HTS power devices design that goes further beyond cryogenic considerations must be accounted in. This is usually the case when BSCCO tapes are used as conductors. Its bending limitations and the presence of flux components perpendicular to tape surface, due to the absence of iron, have to be considered for it may turn some possible applications not so attractive or even practically unfeasible. An all HTS linear synchronous motor built by BSCCO tapes as armature conductors and two trapped-flux YBCO bulks in the mover was constructed and thrust force measurements are starting to be performed. Although the device presents severe restrictions due to the exposed and other reasons, it allowed systematising its design. A pulsed-field magnetiser to generate opposite fluxes for both YBCO bulks is also detailed. Thrust force numerical predictions were already derived and presented.
Fisher, Karl, David J. Lowe, Pedro Tavares, Alice S. Pereira, Boi Hanh Huynh, Dale Edmondson, and William E. Newton. "
{Conformations generated during turnover of the Azotobacter vinelandii nitrogenase MoFe protein and their relationship to physiological function}."
Journal Of Inorganic Biochemistry. 101 (2007): 1649-1656.
AbstractVarious S = 3/2 EPR signals elicited from wild-type and variant Azotobacter vinelandii nitrogenase MoFe proteins appear to reflect different conformations assumed by the FeMo-cofactor with different protonation states. To determine whether these presumed changes in protonation and conformation reflect catalytic capacity, the responses (particularly to changes in electron flux) of the alpha H195Q, alpha H195N, and alpha Q191 K variant MoFe proteins (where His at position 195 in the alpha subunit is replaced by Gln/Asn or Gln at position alpha-191 by Lys), which have strikingly different substrate-reduction properties, were studied by stopped-flow or rapid-freeze techniques. Rapid-freeze EPR at low electron flux (at 3-fold molar excess of wild-type Fe protein) elicited two transient FeMo-cofactor-based EPR signals within 1 s of initiating turnover under N-2 with the alpha H195Q and alpha H195N variants, but not with the alpha Q191K variant. No EPR signals attributable to P cluster oxidation were observed for any of the variants under these conditions. Furthermore, during turnover at low electron flux with the wild-type, alpha H195Q or alpha H195N MoFe protein, the longer-time 430-nm absorbance increase, which likely reflects P cluster oxidation, was also not observed (by stopped-flow spectrophotometry); it did, however, occur for all three MoFe proteins under higher electron flux. No 430-nm absorbance increase occurred with the alpha Q191K variant, not even at higher electron flux. This putative lack of involvement of the P cluster in electron transfer at low electron flux was confirmed by rapid-freeze Fe-57 Mossbauer spectroscopy, which clearly showed FeMo-factor reduction without P cluster oxidation. Because the wild-type, alpha H195Q and alpha H195N MoFe proteins can bind N-2, but alpha Q195K cannot, these results suggest that P cluster oxidation occurs only under high electron flux as required for N-2 reduction. (C) 2007 Elsevier Inc. All rights reserved.