Plasma-induced damage (PID) during plasma-etching processes was suppressed by the application of Cl 2 plasma etching at an optimal temperature of 400°C, based on results of evaluations of photoluminescence (PL), stoichiometric composition, and surface roughness. The effects of ions, photons, and radicals on damage formation were separated from the effects of plasma using the pallet for plasma evaluation (PAPE) method. The PID was induced primarily by energetic ion bombardments at temperatures lower than 400°C and decreased with increasing temperature. Irradiations by photons and radicals were enhanced to form the PID and to develop surface roughness at temperatures higher than 400°C. Consequently, Cl 2 plasma etching at 400°C resulted optimally in low damage and a stoichiometric and smooth GaN surface.
The minimization of plasma-induced damage (PID) in plasma etching is important for the precise and smooth removal of a depth of approximately 7 nm of GaN films to fabricate gate-recess GaN-based normally-off power electronic devices. We have systematically studied the photoluminescence (PL) properties and surface morphologies of GaN films exposed to Cl2 plasma at 400 °C, focusing on their dependences on etch time and ion energy. It is noticeable that PL degradation saturated at etch times of more than 2 min, while surface roughness increased continuously with etch time. Variations of surface roughness with bias voltage were negligible. PID was successfully suppressed by reducing bias voltage, leading to the decrease in incident ion energy on the surface, and thus the near-band-edge emission (NBE) intensity as a PL property was increased to 98.8% of the initial value.
Deep ultraviolet (UV) photons emitted from Cl2 plasmas become a critical cause of degradation in both photoluminescence (PL) properties and surface stoichiometry as a result of plasma-induced damage on GaN films in Cl2 plasma etching at high temperatures. The damages were formed thermally by photon-irradiations of plasma UV emissions with wavelengths of ∼258–306 nm from Cl2 plasma at temperatures greater than 500 °C. The damage were observed with a depth of approximately 3.2 nm. The PL property degraded by the UV emission-induced damage at an early period of plasma etching and reached a constant value.
Surface chemical reactions on the GaN surface with Cl radicals are thermally enhanced in the high-temperature Cl2 plasma etching of GaN, resulting in the formation of etch pits and thereby, a roughened surface. Simultaneous irradiation of ultraviolet (UV) photons in Cl2 plasma emissions with wavelengths of 258 and 306 nm reduces the surface chemical reactions because of the photodissociation of both Ga and N chlorides, which leads to a suppression of the increase in surface roughness. Compared with Si-related materials, we point out that photon-induced reactions should be taken into account during the plasma processing of wide-bandgap semiconductors.
Mitochondrial DNA encodes key subunits of the oxidative phosphorylation complexes essential for ATP production. Translation initiation in mitochondria requires two general factors, mtIF2 and mtIF3, whose counterparts in bacteria are essential for protein synthesis. In this study, we report the characterization of the fission yeast Schizosaccharomyces pombe mtIF2 (Mti2) and mtIF3 (Mti3). Deletion of mti2 impairs cell growth on the respiratory medium. The growth defect of the mti2 deletion mutant can be suppressed by expressing IFM1, the Saccharomyces cerevisiae homolog of Mti2, demonstrating functional conservation between the two proteins. Deletion of mti2 also impairs mitochondrial protein synthesis. Unlike mti2, deletion of mti3 does not affect cell growth on respiratory media and mitochondrial translation. However, deletion of mti3 exacerbates the growth defect of the Δmti2 mutant, suggesting that the two proteins have distinct, but partially overlapping functions during the process of mitochondrial translation initiation in S. pombe. Both Mti2 and Mti3 are associated with the small subunit of the mitochondrial ribosome (mitoribosome). Disruption of mti2, but not mti3, causes dissociation of the mitoribosome and also abolishes Mti3 binding to the small subunit of the mitoribosome. Our results suggest that Mti2 and Mti3 bind in a sequential manner to the small subunit of the mitoribosome and that Mti3 facilitates the function of Mti2 in mitochondrial translation initiation. Our findings also support the view that the importance of the mitochondrial translation initiation factors varies among the organisms.
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