Examinando por Autor "Valenzuela-Ibaceta, Felipe"
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Ítem Biosynthesis of Cu-In-S Nanoparticles by a Yeast Isolated from Union Glacier, Antarctica: A Platform for Enhanced Quantum Dot-Sensitized Solar Cells(MDPI, 2024-03-04) Arriaza-Echanes, Carolina; Campo-Giraldo, Jessica L.; Valenzuela-Ibaceta, Felipe; Ramos-Zúñiga, Javiera; Pérez-Donoso, José M.In recent years, the utilization of extremophile microorganisms for the synthesis of metal nanoparticles, featuring enhanced properties and diverse compositions, has emerged as a sustainable strategy to generate high-quality nanomaterials with unique characteristics. Our study focuses on the biosynthesis of Cu-In-S (CIS) nanoparticles, which has garnered considerable attention in the past decade due to their low toxicity and versatile applications in biomedicine and solar cells. Despite this interest, there is a notable absence of reports on biological methods for CIS nanoparticle synthesis. In this research, three yeast species were isolated from soil samples in an extreme Antarctic environment—Union Glacier, Ellsworth Mountains. Among these isolates, Filobasidium stepposum demonstrated the capability to biosynthesize CIS nanoparticles when exposed to copper sulfate, indium chloride, glutathione, and cysteine. Subsequent purification and spectroscopic characterization confirmed the presence of characteristic absorbance and fluorescence peaks for CIS nanoparticles at 500 and 650 nm, respectively. Transmission electron microscopy analysis revealed the synthesis of monodisperse nanoparticles with a size range of 3–5 nm. Energy dispersive X-ray spectroscopy confirmed the composition of the nanoparticles, revealing the presence of copper, indium, and sulfur. The copper/indium ratio ranged from 0.15 to 0.27, depending on the reaction time. The biosynthesized CIS nanoparticles showed higher photostability than biomimetic nanoparticles and demonstrated successful application as photosensitizers in quantum dot-sensitized solar cells (QDSSC), achieving a conversion efficiency of up to 0.0247%. In summary, this work presents a cost-effective, straightforward, and environmentally friendly method for CIS nanoparticle synthesis. Furthermore, it constitutes the first documented instance of a biological procedure for producing these nanoparticles, opening avenues for the development of environmentally sustainable solar cells.Ítem Steady State Kinetics for Enzymes with Multiple Binding Sites Upstream of the Catalytic Site(MDPI, 2024-12-12) Osorio, Manuel I.; Petrache, Mircea; Salinas, Dino G.; Valenzuela-Ibaceta, Felipe; González-Nilo, Fernando; Tiznado, William; Pérez-Donoso, José M.; Bravo, Denisse; Yáñez, OsvaldoThe Michaelis–Menten mechanism, which describes the binding of a substrate to an enzyme, is a simplification of the process on a molecular scale. A more detailed model should include the binding of the substrate to precatalytic binding sites (PCBSs) prior to the transition to the catalytic site. Our work shows that the incorporation of PCBSs, in steady-state conditions, generates a Michaelis–Menten-type expression, in which the kinetic parameters KM and Vmax adopt more complex expressions than in the model without PCBSs. The equations governing reaction kinetics can be seen as generalized symmetries, relative to time translation actions over the state space of the underlying chemical system. The study of their structure and defining parameters can be interpreted as looking for invariants associated with these time evolution actions. The expression of (Formula presented.) decreases as the number of PCBSs increases, while (Formula presented.) reaches a minimum when the first PCBSs are incorporated into the model. To evaluate the trend of the dynamic behavior of the system, numerical simulations were performed based on schemes with different numbers of PCBSs and six conditions of kinetic constants. From these simulations, with equal kinetic constants for the formation of the Substrate/PCBS complex, it is observed that (Formula presented.) and (Formula presented.) are lower than those obtained with the Michaelis–Menten model. For the model with PCBSs, the (Formula presented.) reaches a minimum at one PCBS and that value is maintained for all of the systems evaluated. Since (Formula presented.) decreases with the number of PCBSs, the catalytic efficiency increases for enzymes fitting this model. All of these observations are consistent with the general equation obtained. This study allows us to explain, on the basis of the PCBS to (Formula presented.) and (Formula presented.) ratios, the effect on enzyme parameters due to mutations far from the catalytic site, at sites involved in the first enzyme/substrate interaction. In addition, it incorporates a new mechanism of enzyme activity regulation that could be fundamental to search for new activity-modulating sites or for the design of mutants with modified enzyme parameters.