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Apoptosis is a highly regulated form of programmed cell death, essential to the development and homeostasis of multicellular organisms. Cytochrome c is a central figure in the activation of the apoptotic intrinsic pathway, thereby activating the caspase cascade through its interaction with Apaf-1. Our recent studies have revealed 14-3-3ε (a direct inhibitor of Apaf-1) as a cytosolic cytochrome c target. Here we explore the cytochrome c / 14-3-3ε interaction and show the ability of cytochrome c to block 14-3-3ε-mediated Apaf-1 inhibition, thereby unveiling a novel function for cytochrome c as an indirect activator of caspase-9/3. We have used calorimetry, NMR spectroscopy, site mutagenesis and computational calculations to provide an insight into the structural features of the cytochrome c / 14-3-3ε complex. Overall, these findings suggest an additional cytochrome c -mediated mechanism to modulate apoptosome formation, shedding light onto the rigorous apoptotic regulation network.

Despite the importance of electron transfer between redox proteins in photosynthesis and respiration, the inter-protein electron transfer rate between redox partner proteins has never been measured as a function of their separation in aqueous solution. Here, we use electrochemical tunneling spectroscopy to show that the current between two protein partners decays along more than 10 nm in the solution. Molecular dynamics simulations reveal a reduced ionic density and extended electric field in the volume confined between the proteins. The distance-decay factor and the calculated local barrier for electron transfer are regulated by the electrochemical potential applied to the proteins. Redox partners could use electrochemically gated, long distance electron transfer through the solution in order to conciliate high specificity with weak binding, thus keeping high turnover rates in the crowded environment of cells. Electron transport chains rely on interactions between redox proteins, but the distance-dependence of the electron transfer rate through the solution is unknown. Here, the authors show that the current between two redox protein partners occurs at long distances and is electrochemically gated.

En la formación universitaria la escritura científico-académica es clave para la elaboración de Trabajos de Fin de Grado o Diplomatura. No obstante, existe un gran vacío en la investigación pedagógica sobre recursos tecnológicos valiosos para el desarrollo de estas competencias. Esta aportación pretende mostrar científicamente la incidencia de la enseñanza mediante un software específico (Scientific Writing Skills) en la mejora de las competencias de escritura científicoacadémica. El estudio se lleva a cabo con 145 estudiantes de Ingeniería en Ciencias Informáticas de la Universidad de las Ciencias Informáticas de La Habana (Cuba). Una vez identificadas las necesidades formativas que los estudiantes perciben para la elaboración de textos científico-académicos, se aplica un diseño experimental pretest y postest para contrastar el efecto del modelo de formación técnico-pedagógico diseñado específicamente para mejorar la competencia de escritura científico-académica. El diseño tecnológico permitió recoger datos de forma automatizada para contrastar las hipótesis de investigación. Los resultados muestran que los estudiantes que hacen uso del modelo experimentado obtienen mejoras significativas en cuanto a la capacidad de redacción de títulos, elaboración de resúmenes, selección de palabras clave, elaboración de bibliografía, redacción del problema y objetivos de investigación, así como elaboración de conclusiones y recomendaciones. Estos resultados son una muestra del potencial de las tecnologías para desarrollar competencias de escritura científico-académicas en la formación universitaria.

Detecting imported diseases by migrants and individuals visiting friends and relatives (VFR) is key in the prevention and management of emergent infectious diseases acquired abroad. Retrospective descriptive study on migrants and VFR from Central and South America between 2017 and 2022 attended at a National Referral Centre for Tropical Diseases in Madrid, Spain. Demographic characteristics, syndromes and confirmed travel-related diagnoses were obtained from hospital patient medical records. 1654 cases were registered, median age of 42 years, 69.1% were female, and 55.2% were migrants. Most cases came from Bolivia (49.6%), followed by Ecuador (12.9%). Health screening while asymptomatic (31.6%) was the main reason for consultation, followed by Chagas disease follow-up (31%). Of those asymptomatic at screening, 47,2% were finally diagnosed of any disease, mainly Chagas disease (19,7%) and strongyloidiasis (10,2%) Our study emphasizes the importance of proactive health screening to detect asymptomatic conditions in migrants and VFR, enabling timely intervention and improved health outcomes. By understanding the unique health profiles of immigrant populations, targeted public health interventions can be devised to safeguard the well-being of these vulnerable groups.

As a not‐for‐profit open access journal, FEBS Open Bio is proud to support the scientific community not only through the publication of open access articles available to all but also through the charitable activities of FEBS. In this editorial, we look back at some of the highlights of the past year and look forward to the new initiatives planned for 2026—all aimed at supporting our community, the scientific community.

In celebration of the 10th anniversary of FEBS Open Bio, we spoke to some of the key figures of the journal's genesis, development, and its future direction, and recount here their thoughts and experiences. Prof. Félix. Goñi discusses the role of the FEBS Publication Committee in the journal's beginnings, Dr Mary Purton relates her experiences as the journal's Executive Editor, Prof. László Fésüs explains how the journal developed during his tenure as Chair of the Publication Committee, and Prof. Johannes Buchner looks forward to the future of FEBS Press and academic publishing. Finally, Prof. John (Iain) Mowbray describes his \"Friday afternoon thought\" to start a new journal.

FEBS Open Bio remains dedicated to serving the scientific community by ensuring rapid publication of rigorous science and pioneering initiatives to support researchers. In this editorial, we reflect on a year of achievements, and look forward to the new developments planned for 2025.

Cardiolipin oxidation and degradation by different factors under severe cell stress serve as a trigger for genetically encoded cell death programs. In this context, the interplay between cardiolipin and another mitochondrial factor—cytochrome c—is a key process in the early stages of apoptosis, and it is a matter of intense research. Cytochrome c interacts with lipid membranes by electrostatic interactions, hydrogen bonds, and hydrophobic effects. Experimental conditions (including pH, lipid composition, and post-translational modifications) determine which specific amino acid residues are involved in the interaction and influence the heme iron coordination state. In fact, up to four binding sites (A, C, N, and L), driven by different interactions, have been reported. Nevertheless, key aspects of the mechanism for cardiolipin oxidation by the hemeprotein are well established. First, cytochrome c acts as a pseudoperoxidase, a process orchestrated by tyrosine residues which are crucial for peroxygenase activity and sensitivity towards oxidation caused by protein self-degradation. Second, flexibility of two weakest folding units of the hemeprotein correlates with its peroxidase activity and the stability of the iron coordination sphere. Third, the diversity of the mode of interaction parallels a broad diversity in the specific reaction pathway. Thus, current knowledge has already enabled the design of novel drugs designed to successfully inhibit cardiolipin oxidation.

Skeletal muscle is more resilient to ischemia-reperfusion injury than other organs. Tissue specific post-translational modifications of cytochrome c (Cyt c ) are involved in ischemia-reperfusion injury by regulating mitochondrial respiration and apoptosis. Here, we describe an acetylation site of Cyt c , lysine 39 (K39), which was mapped in ischemic porcine skeletal muscle and removed by sirtuin5 in vitro. Using purified protein and cellular double knockout models, we show that K39 acetylation and acetylmimetic K39Q replacement increases cytochrome c oxidase (COX) activity and ROS scavenging while inhibiting apoptosis via decreased binding to Apaf-1, caspase cleavage and activity, and cardiolipin peroxidase activity. These results are discussed with X-ray crystallography structures of K39 acetylated (1.50 Å) and acetylmimetic K39Q Cyt c (1.36 Å) and NMR dynamics. We propose that K39 acetylation is an adaptive response that controls electron transport chain flux, allowing skeletal muscle to meet heightened energy demand while simultaneously providing the tissue with robust resilience to ischemia-reperfusion injury. The authors report that acetylation of cytochrome c on K39 acts as a molecular switch in ischemic skeletal muscle, but not other tissues, to increase respiration and prevent apoptosis. This gives skeletal muscle robust resilience to ischemia and ischemia-reperfusion injury.

It has been recently shown that electron transfer between mitochondrial cytochrome c and the cytochrome c 1 subunit of the cytochrome bc 1 can proceed at long-distance through the aqueous solution. Cytochrome c is thought to adjust its activity by changing the affinity for its partners via Tyr48 phosphorylation, but it is unknown how it impacts the nanoscopic environment, interaction forces, and long-range electron transfer. Here, we constrain the orientation and separation between cytochrome c 1 and cytochrome c or the phosphomimetic Y48 p CMF cytochrome c , and deploy an array of single-molecule, bulk, and computational methods to investigate the molecular mechanism of electron transfer regulation by cytochrome c phosphorylation. We demonstrate that phosphorylation impairs long-range electron transfer, shortens the long-distance charge conduit between the partners, strengthens their interaction, and departs it from equilibrium. These results unveil a nanoscopic view of the interaction between redox protein partners in electron transport chains and its mechanisms of regulation. Electron transfer between mitochondrial cytochrome c and subunit of cytochrome bc 1 can proceed at long distance. Here the authors investigate further the mechanism and show phosphorylation regulation of the interactions between the protein partners in the electron transport chain.