Pina, João, Mário Ventim Neves, Alfredo Álvarez, and Amadeu Leão Rodrigues. "
Numerical Design Methodology for an All Superconducting Linear Synchronous Motor."
Technological Innovation for Sustainability. Vol. 349. IFIP Advances in Information and Communication Technology, 349. 2011. 553-562.
AbstractOne potential advantage of the application of superconducting materials in electrical machines is the possibility to build lighter and compact devices by removing iron. These machines find applications, e.g., in systems where cryogenics is already available, or in naturally cryogenic environments. The design of motors with high temperature superconductors (HTS) presents issues unconsidered in classical machines, besides considerations on cryogenics, such as HTS brittleness or mechanical restrictions. Moreover, HTS' electromagnetic properties also degrade due to flux density components, which arise if there is no iron to guide magnetic flux. Several aspects must thus be considered in the design stage, as applications may turn less attractive or even unfeasible. In this paper these issues are detailed, and a numerical methodology for the design of an all superconducting (without iron or conventional conductors) linear synchronous motor is presented.
Timoteo, Cristina G., Alice S. Pereira, Carlos E. Martins, Sunil G. Naik, Americo G. Duarte, Jose J. G. Moura, Pedro Tavares, Boi Hanh Huynh, and Isabel Moura. "
{Low-Spin Heme b(3) in the Catalytic Center of Nitric Oxide Reductase from Pseudomonas nautica}."
Biochemistry. 50 (2011): 4251-4262.
AbstractRespiratory nitric oxide reductase (NOR) was purified from membrane extract of Pseudomonas (Ps.) nautica cells to homogeneity as judged by polyacrylamide gel electrophoresis. The purified protein is a heterodimer with subunits of molecular masses of 54 and 18 kDa. The gene encoding both subunits was cloned and sequenced. The amino acid sequence shows strong homology with enzymes of the cNOR class. Iron/heme determinations show that one heme c is present in the small subunit (NORC) and that approximately two heme b and one non-heme iron are associated with the large subunit (NORB), in agreement with the available data for enzymes of the cNOR class. Mossbauer characterization of the as-purified, ascorbate-reduced, and dithionite-reduced enzyme confirms the presence of three heme groups (the catalytic heme b(3) and the electron transfer heme b and heme c) and one redox-active non-heme Fe (Fe-B). Consistent with results obtained for other cNORs, heme c and heme b in Ps. nautica cNOR were found to be low-spin while FeB was found to be high-spin. Unexpectedly, as opposed to the presumed high-spin state for heme b(3), the Mossbauer data demonstrate unambiguously that heme b(3) is, in fact, low-spin in both ferric and ferrous states, suggesting that heme b(3) is six-coordinated regardless of its oxidation state. EPR spectroscopic measurements of the as-purified enzyme show resonances at the g similar to 6 and g similar to 2-3 regions very similar to those reported previously for other cNORs. The signals at g = 3.60, 2.99, 2.26, and 1.43 are attributed to the two charge-transfer low-spin ferric heme c and heme b. Previously, resonances at the g similar to 6 region were assigned to a small quantity of uncoupled high-spin Fe-III heme b(3). This assignment is now questionable because heme b(3) is low-spin. On the basis of our spectroscopic data, we argue that the g = 6.34 signal is likely arising from a spin spin coupled binuclear center comprising the low-spin Fe-III heme b(3) and the high-spin Fe-B(III). Activity assays performed under various reducing conditions indicate that heme b(3) has to be reduced for the enzyme to be active. But, from an energetic point of view, the formation of a ferrous heme-NO as an initial reaction intermediate for NO reduction is disfavored because heme [FeNO](7) is a stable product. We suspect that the presence of a sixth ligand in the Fe-II-heme b(3) may weaken its affinity for NO and thus promotes, in the first catalytic step, binding of NO at the Fe-B(II) site. The function of heme b(3) would then be to orient the Fe-B-bound NO molecules for the formation of the N-N bond and to provide reducing equivalents for NO reduction.