Resultados de investigación

Desarrollo tecnológico para determinar de forma cuantitativa, durante el tratamiento alcalino en NaOH (cocido) de aceitunas verdes al estilo sevillano, el porcentaje de penetración de la sosa en la pulpa y predecir el momento óptimo para finalizar el proceso. El sistema combina un protocolo de toma de muestras y acondicionamiento del fruto (corte, marcado con fenolftaleína y captura de imagen con iluminación constante) con algoritmos de visión artificial que calculan el porcentaje de cocido. A partir de la serie temporal de medidas, un interpolador estima el instante en el que se alcanzará un umbral objetivo (p.ej., 2/3 o 3/4 de penetración). Incluye además una aplicación web para gestión y trazabilidad del proceso (cloud computing) y evidencia de implantación industrial (TRL 9)., Estructura principal: - Cocido_aceitunas.docx: memoria descriptiva del desarrollo tecnológico (objetivo, descripción, impacto, evidencias). - Cocido Aceitunas.pptx: presentación técnica (metodología y resultados de ensayos). - Patente/3_ES-2394821_B2.pdf: patente antecedente (OEPM) ES-2394821 B2. - Contrato/CONTRATO.pdf: evidencia contractual FIUS–Pymesuma S.L. (23/07/2014) [contiene datos personales]. - Contrato/Contrato FIUS.txt: enlace a proyecto asociado (SISIUS idproy=26626). - README_*: ficheros de descripción para depósito en repositorio.

Post-translational modifications and naturally occurring mutations of cytochrome c have been recognized as a regulatory mechanism to control its biology. In this work, we investigate the effect of such in vivo chemical modifications of human cytochrome c on its redox properties in the adsorbed state onto an electrode. In particular, tyrosines 48 and 97 have been replaced by the non-canonical amino acid p-carboxymethyl-L-phenylalanine (pCMF), thus mimicking tyrosine phosphorylation. Additionally, tyrosine 48 has been replaced by a histidine producing the natural Y48H pathogenic mutant. Thermodynamics and kinetics of the interfacial electron transfer of wild-type cytochrome c and herein produced variants, adsorbed electrostatically under different local interfacial electric fields, were determined by means of variable temperature cyclic film voltammetry. It is shown that non-native cytochrome c variants immobilized under a low interfacial electric field display redox thermodynamics and kinetics similar to those of wild-type cytochrome c. However, upon increasing the strength of the electric field, the redox thermodynamics and kinetics of the modified proteins markedly differ from those of the wild-type species. The mutations promote stabilization of the oxidized form and a significant increase in the activation enthalpy values that can be ascribed to a subtle distortion of the heme cofactor and/or difference of the amino acid rearrangements rather than to a coarse protein structural change. Overall, these results point to a combined effect of the single point mutations at positions 48 and 97 and the strength of electrostatic binding on the regulatory mechanism of mitochondrial membrane activity, when acting as a redox shuttle protein., File name: Otras-figuras_Ms_BBA-Bioenergetics.docx Description: A Word file with the figure images File name: Raw_data.zip Description: .nox files with the raw data of voltammetry File name: Fig_2+3+6.jnb Description: A sigmaplot file with figures 2+3+6 File name: Fig_5.jnb Description: A sigmaplot file with figure 5

Surface reconstituted metal-organic frameworks (MOFs) offer appealing properties for electrocatalysis due to their unique structural and compositional advantages. In this work, a controlled potential-induced reconstruction of a two-dimensional cobalt metal-organic framework for boosting oxygen evolution reaction in alkaline media is reported. The current MOF is shown to undergo a partial structural transformation that generates a heterogeneous system, where the original MOF coexists with an oxyhydroxide phase. In fact, the potential-induced stabilization of Co(III) metal centers in the MOF is crucial for delaying its full degradation in alkaline media. This partial retention of the Co(III)MOF phase in the so-derived heterogeneous catalyst has been demonstrated to be decisive for boosting the alkaline electrocatalytic oxygen evolution reaction (OER), displaying superior OER activity in terms of both thermodynamic and kinetic merits compared to the benchmark IrO2 and RuO2 electrocatalysts and the prototypical cobalt (oxy)hydroxides, with a Tafel slope of 52 mV dec−1 and a turnover frequency (TOF) of 6.8 s−1 at 450 mV. Remarkably, the generated final product is stable, exhibiting high robustness and long durability for long-term OER electrolysis. This work provides new insight into the impact of the reconstruction of a MOF for alkaline OER under typical electrochemical conditions, which ultimately benefits the rational design of MOF-based catalysts with high electrocatalytic activity for oxidation reactions., File name: Otras-figuras_Ms_Catalysis-today.docx Description: A Word file with the figure images File name: Raw_data.zip Description: .nox files with the raw data of voltammetry File name: Fig_4.jnb Description: A sigmaplot file with figure 4. File name: Fig_5.jnb Description: A sigmaplot file with figure 5. File name: Fig_6.jnb Description: A sigmaplot file with figure 6. File name: Fig_7.jnb Description: A sigmaplot file with figure 7. File name: Fig_-2a,b.jnb Description: A sigmaplot file with figure 2.

Protein film voltammetry is a sensitive tool to characterize the electron transfer properties of redox proteins in a variety of environments and conformational states. Here, a detailed voltammetric study aimed to explore the effect of electrostatic immobilization on the electron transfer thermodynamics and kinetics of adsorbed human- and horse- cytochrome c was carried out. For this purpose, the two cytochromes were adsorbed on thiol monolayers (SAM) with different immobilization strengths and donor–acceptor distances. While thermodynamic redox parameters do not seem to be affected by the monolayer thickness and charge density, electron transfer kinetics are significantly modulated by the protein immobilization strength. Stronger protein–SAM electrostatic interactions result in lower electron transfer rates in both non-adiabatic and friction kinetic regimes. This behavior is further characterized by smaller pre-exponential factors and activation enthalpies in Arrhenius type plots. These kinetic results in the physiologically relevant non-adiabatic electron transfer regime are shown to be consistent with the recently developed Matyushov’s theoretical formulation of protein electron transfer. Moreover, a comparison between the kinetic parameters of the two cytochrome variants supports the hypothesis that differences between their electron transfer rates originate in their structural flexibility to accommodate the conformational changes required to form the precursor complex between cytochrome and a negatively charged redox partner., File name: Figuras_JEAC_2025.docx Description: A Word file with the figure images File name: Figuras.zip Description: A sigmaplot files with the figures File name: Raw_Data.zip Description: .nox files with the raw data

Metal-organic frameworks (MOFs) can be used as precursors for the directed synthesis of derived materials with enhanced performance for electrocatalysis. Herein, we report on an in-situ electrochemical strategy for the selective synthesis of hybrid electrocatalysts using a cobalt MOF (2D-CoMOF) as a precursor for constructing electrochemical sensors to monitor the glucose oxidation reaction (GOR). By using in-situ Raman spectroelectrochemistry, it is demonstrated that a precise control of the applied potential during amperometric treatment of 2D-CoMOF can promote the generation of derived heterostructures in which the original MOF coexists with metal oxides and/or oxyhydroxides (MOF-MOx) with different compositions. The so-prepared electrodes exhibit high electroactive surface areas, a high number of electrocatalytically active cobalt sites and an efficient charge transport across the catalytic film. Moreover, their composition-dependent electrocatalytic performance for the glucose oxidation reaction is examined, establishing a relationship between the applied potential, the macroscopic chemical composition of the heterostructure and the electrocatalytic performance for glucose sensing. In particular, the hybrid phases consisting of Co-MOF/Co3O4/CoOOH display superior electrocatalytic sensing performance with a wide linear concentration range and high sensitivity. The present work emphasizes the significance that the precise control of the applied potential has on the electrochemically-assisted MOF transformation for developing highly efficient MOF-derived electrocatalysts.

Metal–organic frameworks (MOFs) are attractive porous materials for electrocatalytic applications associated with carbon-free energy storage and conversion. This type of material usually requires a post-treatment to be used as electrocatalyst. The present work comprehensively investigates the electrochemical activation of a cobalt-MOF@Nafion composite that produces outstanding electrocatalytic performance for the water oxidation reaction at neutral pH. A detailed electrochemical characterization reveals that the electroactivation of the composite requires the participation of the oxygen evolution reaction (OER) and leads to a significant increase in the electroactive population of cobalt centers. It is shown that an increase of the applied activation potential in the OER region results in a faster electroactivation of the Co-MOF without affecting the intrinsic electrocatalytic properties of the active cobalt centers, as evidenced by the unique linear correlation between the electrocatalytic OER current and the population of electroactive cobalt. In addition, at structural level, it is shown that the electrochemical activation causes the partial disruption of the Nafion adlayer, as well as morphological changes of the Co–MOF particles from a compact, rounded morphology, before electrochemical activation, to a more open and expanded structure, after electroactivation; with the concomitant increase of the number of surface–exposed cobalt centers. Interestingly, these cobalt centers retain their coordinative chemistry and their laminar distribution in the nanosheets at the nanoscale, which is consistent with the preservation of their intrinsic electrocatalytic activity after potential–induced activation. In this scenario, these results suggest that only the electroactivated cobalt centers with good accessibility to the electrolyte are electrochemically active. This work provides a better understanding of the processes and structural changes underlying the electrochemical activation at neutral pH of a Co–MOF for boosting the electrocatalytic water oxidation reaction., File name:ASS_2023_Olloqui_Figuras.docx Description: A Word file with the figure images File name:Figure_1.jnb Description: A sigmaplot file with figure 1. File name:Figure_2.jnb Description: A sigmaplot file with figure 2. File name: Raw_data.zip Description: .nox files with the raw data of voltammetry

Metal-organic frameworks (MOFs) are receiving increased attention as new functional nanomaterials for the development of electrochemical sensors. Herein, we develop an electrochemical platform for non-enzymatic hydrogen peroxide detection built with a composite of two-dimensional cobalt MOF nanosheets and Nafion (2D-Co-MOF@Nafion). The feasibility of the 2D-Co-MOF@Nafion composite as active material for high performance hydrogen peroxide sensor was investigated by using cyclic voltammetry and chronoamperometry. Its voltammetric response reveals an efficient charge transport through the MOF composite, and rapid electron exchange between MOF and electrode. Notably, these MOF nanosheets exhibit enzyme-like activity for the non-common catalytic oxidation of hydrogen peroxide, leading to an electrochemical sensor with rapid quantitative detection, outstanding sensitivity, selectivity, stability, and durability at the desirable neutral pH. In particular, for a cobalt metal loading of 1.2 nanomol, the sensor yields amperometric H2O2 detection with characteristic electrocatalytic parameters of imax= 5.7 mA cm−2 and KM = 13 mM. Moreover, linear ranges of up to either 1 mM or 10 mM are achieved, with sensitivities as high as 570 ± 5 A cm−2 mM−1 or 395 ± 10 A cm−2 mM−1 for the low and high concentration ranges, respectively. The particular coordination chemistry of the MOF consisting of a regular arrangement of multiple Co(II) redox metal sites connected by appropriate organic ligands can provide inherent enzyme-mimicking properties, thereby explaining the higher oxidase-like activity of the present MOF. This work raises the new idea of using two-dimensional cobalt-based MOFs as active nanozymes, offering exciting opportunities in the design of non-enzymatic electrochemical sensing devices., File name: raw data.zip Description: .ocw files with the raw data File name: ASS_2023_Olloqui_Figuras.docx Description: A Word file with the figure images File name: Figure_2_S4.jnb Description: A sigmaplot file with figures 1 and S4. File name: Figure_3_y_4.jnb Description: A sigmaplot file with figures 3 and 4. File name: Figure_6.jnb Description: A sigmaplot file with figure 6. File name: Figure_S3.jnb Description: A sigmaplot file with figure S3.

Se incluyen datos del Proyecto Pintura, poder, sociedad y naturaleza en el Quito barroco (PID2020-112852GB-I00): bibliografías, relación de instituciones en las que se ha investigado, publicaciones de los miembros del Proyecto vinculadas directamente al mismo, tabla, carteles y programas de actividades desarrolladas desde el Proyecto, A) Bibliografías (PDF): -Bibliografía del Proyecto (PDF) -Bibliografía de la monografía Pintura, poder, sociedad y naturaleza en el Quito barroco (PDF) B) Relación de publicaciones generadas por el Proyecto (PDF) C) Tablas (PDF): -Tabla de las especies citadas en las cartelas de los Tipos de la Real Audiencia de Quito (Salgueiro González 2023) (PDF) D) Relación de instituciones en las que se ha realizado el trabajo de campo del Proyecto (PDF) E) Carteles y programas de las actividades organizadas por el Proyecto (PDF y JPG): -Programa del I Simposio Internacional “Arte, historia y cultura en el Quito virreinal” (PDF) -Programa del II Simposio Internacional “Arte, historia y cultura en el Quito virreinal” (PDF) -Programa del Simposio “Mujeres pintoras y la imagen de la mujer en el Quito barroco” (PDF) -Programa del Taller del Seminario de Investigación en Historia Moderna de América (abril de 2022) (PDF) -Programa del Taller del Seminario de Investigación en Historia Moderna de América (abril de 2023) (PDF) -Programa del Taller del Seminario de Investigación en Historia Moderna de América (junio de 2024) (PDF) -Programa del Congreso “Pintura, poder, sociedad y naturaleza en el Quito barroco”. (PDF) -Cartel de Congreso “Pintura, poder, sociedad y naturaleza en el Quito barroco” (JPG) -Cartel del Simposio “Mujeres pintoras y la imagen de la mujer en el Quito barroco” (JPG) F) Publicaciones en Open Access: Se relacionan las publicaciones en Open Access. Se depositarán en idUS aquellas que cuenten con los correspondientes permisos de las editoriales. Las que pertenecen a editoriales con repositorios en línea, y que ya han publicado investigaciones del Proyecto, son las siguientes: buleria.nileon.es, e-revistes.uji.es, rio.upo.es, journals.uco.es, revistas.icanh.gov.co, editorial.ucuenca.edu.ec Martín Rodríguez, P. (2022). Del dibujo de campo a la lámina botánica: Análisis del proceso de trabajo tras una estampa de la Flora peruviana et chilensis. UCOARTE. Revista De Teoría E Historia Del Arte, 11, 67–82. https://doi.org/10.21071/ucoarte.v11i.14231 Justo Estebaranz, Á., Vásquez Hahn, M. A. y Chiva Beltrán, J. (2025, en prensa). «A fin de acreditar la alegría y congratulación que demanda un asunto tan remarcable»: Fiestas en Quito por la Independencia (1822-1830)". Potestas, nº 26. En prensa. Justo-Estebaranz, Á. (2023). La clave está en el herrero: artesanado local y robos de obras de arte y de útiles de trabajo en Quito durante los siglos XVII y XVIII. En A. Contreras-Guerrero, Á. Justo-Estebaranz, & F. Quiles (Eds.), En las sombras del Barroco. Una mirada introspectiva (pp. 305-337). Publicación Enredars/ Andavira Editora. https://rio.upo.es/rest/api/core/bitstreams/b6e40273-bc09-4cc9-b74e-37067b2b64e1/content Justo-Estebaranz, Á. (2023). El Órgano de la Iglesia del Sagrario de Cuenca: Historia e Iconografía. En Memorias del III Encuentro Nacional de Historia de la Provincia del Azuay (pp. 69-86). Universidad de Cuenca. https://editorial.ucuenca.edu.ec/omp/index.php/ucp/catalog/view/78/235/415 Montes Sánchez, M. y Justo-Estebaranz, Á. (2024). Entre retablos, adulterio y cárcel: el batihoja Vicente Egas en Cuenca. En “Y VERÉIS TODA ESTA ARENA DE CARROS DE PLATA LLENA”. ESTUDIOS SOBRE LA PLATA EN IBEROAMÉRICA De los orígenes al siglo XIX (pp. 799-814). Secretaría de Cultura. INAH. Instituto Nacional de Antropología e Historia Coordinación Nacional de Monumentos Históricos (México), Instituto de Humanismo y Tradición Clásica Universidad de León (España).

Mitochondria play a crucial role in cellular energy production, signaling and homeostasis. Respiratory supercomplexes represent evolutionary well-conserved, stable associations between membrane complexes and molecules, including proteins and lipids, within the inner mitochondrial membrane. They dynamically respond to metabolic demands and enhance the electron transfer rate, thereby reducing the production of ROS. Recent research has unveiled cytochrome c, a mobile electron carrier between complexes III and IV, as a potential key player in orchestrating the formation of these supra-associations. This study centers on elucidating the role of cytochrome c in modulating the assembly of supercomplexes, using the Saccharomyces cerevisiae yeast as a model system for mitochondrial metabolism. BN-PAGE and mass spectrometry-based proteomic analysis were employed to examine supercomplex organization in yeast strains expressing different cytochrome c isoforms, grown under fermentative and respiratory conditions. Our results demonstrate that both isoforms of cytochrome c contribute to supercomplex assembly, with isoform-2 significantly improving electron transfer and lowering ROS levels. We propose a model in which cytochrome c acts as a scaffold for the recruitment of assembly factors, facilitating the formation of higher order supercomplexes such as III2IV2. This model highlights cytochrome c's role beyond electron transfer, as it regulates supercomplex assembly and mitochondrial homeostasis., File name: Otras-figuras_Ms_IJBM.docx Description: A Word file with the figure images File name: Raw_data.zip Description: .nox files with the raw data of voltammetry File name: Fig_2+S5+S6+S7.jnb Description: A sigmaplot file with figures 2+S5+S6+S7

Post-translational modifications (PTMs) of proteins are ubiquitous processes present in all life kingdoms, involved in the regulation of protein stability, subcellular location and activity. In this context, cytochrome c (Cc) is an excellent case study to analyze the structural and functional changes induced by PTMS as Cc is a small, moonlighting protein playing different roles in different cell compartments at different cell-cycle stages. Cc is actually a key component of the mitochondrial electron transport chain (ETC) under homeostatic conditions but is translocated to the cytoplasm and even the nucleus under apoptotic conditions and/or DNA damage. Phosphorylation does specifically alter the Cc redox activity in the mitochondria and the Cc non-redox interaction with apoptosis-related targets in the cytoplasm. However, little is known on how phosphorylation alters the interaction of Cc with histone chaperones in the nucleus. Here, we report the effect of Cc Tyr48 phosphorylation by examining the protein interaction with SET/TAF-Iβ in the nuclear compartment using a combination of molecular dynamics simulations, biophysical and structural approaches such as isothermal titration calorimetry (ITC) and nuclear magnetic resonance (NMR) and in cell proximity ligation assays. From these experiments, we infer that Tyr48 phosphorylation allows a fine-tuning of the Cc-mediated inhibition of SET/TAF-Iβ histone chaperone activity in vitro. Our findings likewise reveal that phosphorylation impacts the nuclear, stress-responsive functions of Cc, and provide an experimental framework to explore novel aspects of Cc post-translational regulation in the nucleus., File name: Figuras_Ms_Protein_science.docx Description: A Word file with the figure images File name: Figure_S6a,b,c.jnb Description: A sigmaplot file with figures S6 File name: Raw_data_061023.zip Description: .nox files with the raw data