To completely characterize the evolving state of a plasma, diagnostic tools that enable measurements of the time-resolved behavior are required. In this study, a gridded ion source with superimposed oscillations was utilized to verify the functionality of a high-speed retarding potential analyzer (HSRPA), at frequencies equivalent to the low frequency oscillations occurring in Hall effect thrusters (HETs). The verification of this device provides an effective alternative to existing diagnostics for measuring time-resolved ion energies. Retarding potential analyzers (RPAs) have established themselves as a fundamental diagnostic in the field of electric propulsion (EP), enabling the measurement of ion energy distributions within the plumes of EP thrusters. The work presented here has demonstrated the capability of a standard RPA in conjunction with high-speed circuitry and data fusion techniques to produce time-resolved ion energy distribution functions (IEDFs) at higher frequencies and beam potentials than have previously been investigated. Tested frequencies ranged between 20 and 80 kHz with 10 V peak-to peak oscillations at a mean beam potential of 570 V. In addition, measurements were conducted with several waveforms, functioning as the superimposed oscillation, including a sine wave, triangle wave, and noisy sine wave. Data from the HSRPA were successfully reconstructed into time series utilizing two data fusion techniques: the empirical transfer function method and shadow manifold interpolation. Time-resolved IEDFs were produced at all frequency set points and waveforms. This investigation has demonstrated the HSRPA effectiveness at producing time-resolved measurements under conditions similar to those occurring in HETs.
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http://dx.doi.org/10.1063/5.0176167 | DOI Listing |
Photosynth Res
January 2025
Department of Chemistry, Graduate School of Science and Technology, Proteo-Science Research Center, Ehime University, Bunkyo-cho, Matsuyama, Ehime, 790-8577, Japan.
The active site for water oxidation in photosystem II (PSII) comprises a MnCaO cluster adjacent to a redox-active tyrosine residue (Tyr). During the water-splitting process, the enzyme transitions through five sequential oxidation states (S to S), with O evolution occurring during the STyr· to STyr transition. Chloride also plays a role in this mechanism.
View Article and Find Full Text PDFJ Fluoresc
January 2025
Department of Chemistry, The University of Burdwan, Golapbag, Burdwan, 713104, India.
Nitrogen doped Carbon Quantum Dots (NCQDs) have been synthesized using most economical and easiest hydrothermal process. Here, N-phenyl orthophenylenediamine and citric acid were utilised as a source of nitrogen and carbon for the preparation of NCQDs. The synthesized NCQDs were characterized using experimental techniques like UV - Vis absorption, FT-IR, transmission electron microscopy (TEM), X-ray Diffraction (XRD), EDX, dynamic light scattering (DLS), fluorimeter and time resolved fluorescence spectroscopy.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
ROS (i.e., reactive oxygen species) scavenging is a key function of various Mn-based enzymes, including superoxide dismutases (SODs) and catalases, which are actively linked to oxidative stress-related diseases.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Shanghai Key Laboratory of Metabolic Remodeling and Health, Institute of Metabolism and Integrative Biology, Fudan University, Shanghai 200438, China.
Chaperone-mediated autophagy (CMA) is a selective autophagic pathway responsible for degrading cytoplasmic proteins within lysosomes. Monitoring CMA flux is essential for understanding its functions and molecular mechanisms but remains technically complex and challenging. In this study, we developed a pH-resistant probe, KFERQ-Gamillus, by screening various green fluorescent proteins.
View Article and Find Full Text PDFCell
January 2025
Department of Molecular and Cell Biology and School of Engineering and Applied Sciences, Harvard University, Cambridge, MA, USA. Electronic address:
Understanding protein function would be facilitated by direct, real-time observation of chemical kinetics in the atomic structure. The selectivity filter (SF) of the K channel provides an ideal model, catalyzing the dehydration and transport of K ions across the cell membrane through a narrow pore. We used a "pump-probe" method called electric-field-stimulated time-resolved X-ray crystallography (EFX) to initiate and observe K conduction in the NaK2K channel in both directions on the timescale of the transport process.
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