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In this study, we analyzed and developed a phosphor with a nitridiosilicate based and emitting color changing from green to orange to apply to our white-light-emitting diodes (WLEDs). Eu2+ and Yb2+ trap sites for twodoped SrSi2O2N2:Eu2+,Yb2+ (SrYb) nitridosilicate emit a wide emission in the region between green and orange. By calculating the decompose time of the green-emission power donor, we could determine the converted energy between the active ions. Furthermore, we also analyzed the impact of codoping with varied active ion ratios on the photoluminescence (PL) characteristics. As the concentration of Yb2+ increases, the red emission dominates the green. This was because the obtained phoshor's emission depended on the activator ion components. To generate white light, a combination containing the acquired phosphor and the indium gallium nitride (InGaN) blue LED chip with 450-nm wavelength was used. With only two steps, we could detect the hue balance management. Firstly, by modifying the Eu2+ and Yb2+ concentrations, we can conduct a green-toorange proportion optimization. Following that, the commission on illumination (CIE) coordinates were transformed to [0.4071; 0.3789] from the original position, which was [0.2805; 0.2014] by enhancing the phosphor powder amount. An environment which has a CRI of around 89 is the optimum condition for conducting white light.

REP, diverse palindromic DNA sequences found at high copy number in many bacterial genomes, have been attributed important roles in cell physiology but their dissemination mechanisms are poorly understood. They might represent non-autonomous transposable elements mobilizable by TnpAREP, the first prokaryotic domesticated transposase associated with REP. TnpAREP, fundamentally different from classical transposases, are members of the HuH superfamily and closely related to the transposases of the IS200/IS605 family. We previously showed that Escherichia coli TnpAREP processes cognate single stranded REP in vitro and that this activity requires the integrity of the REP structure, in particular imperfect palindromes interrupted by a bulge and preceded by a conserved DNA motif. A second group of REPs rather carry perfect palindromes, raising questions about how the latter are recognized by their cognate TnpAREP. To get insight into the importance of REP structural and sequence determinants in these two groups, we developed an in vitro activity assay coupled to a mutational analysis for three different TnpAREP/REP duos via a SELEX approach. We also tackled the question of how the cleavage site is selected. This study revealed that two TnpAREP groups have co-evolved with their cognate REPs and use different strategies to recognize their REP substrates.