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2. A white paper from the FEBS Education and Training Conference: challenges, opportunities, and action plans for transforming molecular life sciences education.

Author

Villo, Ly, Sincic, Nino, Mello, Luciane V., Costa, Manuel Joao, Picard, Didier, Malatesta, Francesco, Dumic, Jerka, and Sagin, Ferhan G.

Subjects
EDUCATION conferences, LIFE science education, TECHNOLOGICAL innovations, SCIENCE conferences, DIGITAL technology
Abstract

The inaugural FEBS Education and Training Conference (ETC) was held in Türkiye, in 2024. This first‐ever Molecular Life Sciences Education Conference in Europe was organized by the FEBS Education and Training Committee and it was a groundbreaking event that brought together educators and scientists to explore how to enhance education and training in molecular life sciences. The conference explored a wide range of critical themes, for example—digital revolution, active learning and student engagement, multidisciplinary teaching and learning, transitions and inclusivity in education, students' self‐assessment, and self‐regulated learning. The discussions and presentations underscored the pressing need for transformation in how academics and researchers approach teaching and learning. Such shift is driven by rapid technological advancements, societal shifts, and the evolving demands of the scientific landscape. This document synthesizes key insights, discussions, and recommendations from the conference and proposes actionable strategies for all stakeholders in the field—institutions, educators and students—to address current challenges in education and training in molecular life sciences. [ABSTRACT FROM AUTHOR]

Published
2025
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21. Fondamenti di biochimica umana

Author

Consalvi, Valerio, Chiaraluce, Roberta, and Malatesta, Francesco

Subjects
biomolecole funzionali e strutturali, biomolecole funzionali e strutturali, biochimica d'organo, biochimica speciale, biochimica d'organo, biochimica speciale
Published
2021

22. Tryptophan 121 of subunit II is the electron entry site to cytochrome-c oxidase in Paracoccus denitrificans. Involvement of a hydrophobic patch in the docking reaction

Author

Witt, Heike, Malatesta, Francesco, Nicoletti, Flavia, Brunori, Maurizio, Ludwig, Bernd, Witt, Heike, Malatesta, Francesco, Nicoletti, Flavia, Brunori, Maurizio, and Ludwig, Bernd

Abstract

To investigate the contribution of hydrophobic residues to the molecular recognition of cytochrome c with cytochrome oxidase, we mutated several hydrophobic amino acids exposed on subunit II of the Paracoccus denitrificans oxidase. KM and kcat values and the bimolecular rate constant were determined under steady- or presteady-state conditions, respectively. We present evidence that Trp-121 which is surrounded by a hydrophobic patch is the electron entry site to oxidase. Mutations in this cluster do not affect the binding of cytochrome c as the KM remains largely unchanged. Rather, the kcat is reduced, proposing that these hydrophobic residues are required for a fine tuning of the redox partners in the initial collisional complex to obtain a configuration optimal for electron transfer.

Published
2021

23. Different interaction modes of two cytochrome-c oxidase soluble CuA fragments with their substrates

Author

Maneg, Oliver, Ludwig, Bernd, Malatesta, Francesco, Maneg, Oliver, Ludwig, Bernd, and Malatesta, Francesco

Abstract

Cytochrome-c oxidase is the terminal enzyme in the respiratory chains of mitochondria and many bacteria and catalyzes the formation of water by reduction of dioxygen. The first step in the cytochrome oxidase reaction is the bimolecular electron transfer from cytochrome c to the homobinuclear mixed-valence CuA center of subunit II. In Thermus thermophilus a soluble cytochrome c552 acts as the electron donor to ba3 cytochrome-c oxidase, an interaction believed to be mainly hydrophobic. In Paracoccus denitrificans, electrostatic interactions appear to play a major role in the electron transfer process from the membrane-spanning cytochrome c552. In the present study, soluble fragments of the CuA domains and their respective cytochrome c electron donors were analyzed by stopped-flow spectroscopy to further characterize the interaction modes. The forward and the reverse electron transfer reactions were studied as a function of ionic strength and temperature, in all cases yielding monoexponential time-dependent reaction profiles in either direction. From the apparent second-order rate constants, equilibrium constants were calculated, with values of 4.8 and of 0.19, for the T. thermophilus and P. denitrificans c552 and CuA couples, respectively. Ionic strength strongly affects the electron transfer reaction in P. denitrificans indicating that about five charges on the protein interfaces control the interaction, when analyzed according to the Brønsted equation, whereas in the T. thermophilus only 0.5 charges are involved. Overall the results indicate that the soluble CuA domains are excellent models for the initial electron transfer processes in cytochrome-c oxidases.

Published
2021

36. Tryptic digestion of soybean lipoxygenase-I generates a 60 kDa fragment with improved activity and membrane binding ability

Author

Maccarrone, Mauro, Salucci, Marie Luisa, Zadelhoff, Guus van, Malatesta, Francesco, Veldink, Gerrit, Vliegenthart, Johannes F.G., and Finazzi-Argo, Alessandro

Subjects
Biochemistry -- Research, Enzymes -- Research, Fatty acids -- Research, Membranes (Biology) -- Research, Biological sciences, Chemistry
Abstract

Research has been conducted on the soybean lipoxygenase-I composed of N-terminal and C-terminal domains. Results suggest that the N-terminal domain is enzyme's built-in inhibitor of catalytic activity and membrane binding ability.

Published
2001

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