The emission localization and blueshift agrees with experimental photoluminescence observations in QWs deposited on textured GaN. Electrostatic shielding of the parallel polar potential by free carriers leads to localized band bending RepSox in vitro at the wedges, instead of uniform band tilting, inducing tighter lateral carrier confinement. Thus the ridges formed by intersecting QWs behave as a network of quantum wires. Since electrons and holes are confined in opposite polarity wedges, separated by a QW length, direct recombination between QWG-trapped electrons and holes is unlikely; instead radiative emission at the wedges

involves recombination between trapped electrons-”"passing”" holes and vice versa. A simplified analytical theory CCI-779 is introduced to obtain the energy levels and the transition probabilities via overlap integrals. The passing-trapped emission

rates are comparable to those for emission in flat QWs, and the blueshift in wavelength is in good agreement with the observed values. (C) 2009 American Institute of Physics. [DOI: 10.1063/1.3187906]“
“In Arabidopsis thaliana, a gene family of six members encodes acyl-CoA-binding proteins (ACBPs). These Arabidopsis ACBPs (designated ACBP1 to ACBP6) range in size from 10.4 kDa to 73.1 kDa and display varying affinities for acyl-CoA esters, suggesting that they have different roles in plant lipid metabolism. SN-38 nmr In contrast, only the 10-kDa ACBPs have been well-characterized from other eukaryote species. Our previous studies have revealed that ACBP1 and ACBP2 are membrane-associated proteins, while ACBP3 is extracellularly-targeted. More recently, we have reported that the remaining three members in this protein family (namely ACBP4, ACBP5 and ACBP6) are subcellularly localized to the cytosol in Arabidopsis. The subcellular localizations of ACBP4, ACBP5 and ACBP6 in the cytosol were demonstrated using a number of different approaches incorporating biochemical fractionation, confocal microscopy of transgenic Arabidopsis expressing autofluorescence-tagged fusions and immunoelectron microscopy using ACBP-specific antibodies. Our results indicate that all

three ACBPs in the cytosol are potential candidates for acyl-CoA binding and trafficking in plant cells. In this review, the functional redundancy and differences among the three cytosolic ACBPs are discussed by comparison of their light-regulated expression and substrate affinities to acyl-CoA esters, and from biochemical analyses on their knockout mutants and/or overexpression in transgenic Arabidopsis. The transcriptionally light-induced ACBP4 and ACBP5, which encode the two largest forms of Arabidopsis ACBPs, bind oleoyl-CoA esters and likely transfer oleoyl-CoAs from the plastids (the site of de novo fatty acid biosynthesis) to the endoplasmic reticulum for the biosynthesis of non-plastidial membrane lipids in Arabidopsis.