Fernandes, M.a, Vieira Martins M. a R. b. "
Modeling the laser scanned photodiode S-shaped J-V characteristic."
Materials Research Society Symposium Proceedings. Vol. 989. 2007. 469-474.
AbstractThe devices analyzed in this work present an S-shape J-V characteristic when illuminated. By changing the light flux a non linear dependence of the photocurrent with illumination is observed. Thus a low intensity light beam can be used to probe the local illumination conditions, since a relationship exists between the probe beam photocurrent and the steady state illumination. Numerical simulation studies showed that the origin of this S-shape lies in a reduced electric field across the intrinsic region, which causes an increase in the recombination losses. Based on this, we present a model for the device consisting of a modulated barrier recombination junction in addition to the p-i-n junction. The simulated results are in good agreement with the experimental data. Using the presented model a good estimative of the LSP signal under different illumination conditions can be obtained, thus simplifying the development of applications using the LSP as an image sensor, with advantages over the existing imaging systems in the large area sensor fields with the low cost associated to the amorphous silicon technology. © 2007 Materials Research Society.
Prabakaran, R., T. Monteiro, M. Peres, A. S. Viana, AF Da Cunha, H. Águas, A. Gonçalves, E. Fortunato, R. Martins, and I. Ferreira. "
Optical and structural analysis of porous silicon coated with GZO films using rf magnetron sputtering."
Thin Solid Films. 515.24 (2007): 8664-8669.
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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.