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Structural insights into the role of the prosegment binding loop in a papain-superfamily cysteine protease from Treponema denticola.

Acta Crystallogr F Struct Biol Commun

February 2025

Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, State University of New York, Buffalo, New York, USA.

Periodontal diseases afflict 20-50% of the global population and carry serious health and economic burdens. Chronic periodontitis is characterized by inflammation of the periodontal pocket caused by dysbiosis. This dysbiosis is coupled with an increase in the population of Treponema denticola, a spirochete bacterium with high mobility and invasivity mediated by a number of virulence factors.

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Dissecting the biophysical mechanisms of oleate hydratase association with membranes.

Front Mol Biosci

January 2025

Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, KY, United States.

This study investigates the dynamics of oleate hydratase (OhyA), a bacterial flavoenzyme from , and its interactions with lipid membranes, focusing on the factors influencing membrane binding and oligomerization. OhyA catalyzes the hydration of unsaturated fatty acids, playing a key role in bacterial pathogenesis by neutralizing host antimicrobial fatty acids. OhyA binds the membrane bilayer to access membrane-embedded substrates for catalysis, and structural studies have revealed that OhyA forms oligomers on membrane surfaces, stabilized by both protein-protein and protein-lipid interactions.

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Activity and stability origin of core-shell catalysts: unignorable atomic diffusion behavior.

Chem Sci

January 2025

Interdisciplinary Research Center for Sustainable Energy Science and Engineering (IRC4SE2), School of Chemical Engineering, Zhengzhou University Henan 450001 China

The exceptional oxygen reduction reaction (ORR) and oxygen evolution reaction (OER) performances of core-shell catalysts are well documented, yet their activity and durability origins have been interpreted only based on the static structures. Herein we employ a NiFe alloy coated with a nitrogen-doped graphene-based carbon shell (NiFe@NC) as a model system to elucidate the active structure and stability mechanism for the ORR and OER by combining constant potential computations, molecular dynamic simulations, and experiments. The results reveal that the synergistic effects between the alloy core and carbon shell facilitate the formation of Fe-N-C active sites and replenish metal sites when central metal atoms detach.

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Hydrothermal carbonization (HTC) of carbohydrates has been reported as a sustainable and green technique to produce carbonaceous micro- and nano-materials. These materials have been developed for several applications, including catalysis, separation science, metal ion adsorption and nanomedicine. Carbon nanoparticles (CNPs) obtained through HTC are particularly interesting for the latter application since they exhibit photothermal properties when irradiated with near-infrared (NIR) light, act as an antioxidant by scavenging reactive oxygen species (ROS), and present good colloidal stability and biocompatibility.

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OaPAC, the photoactivated adenylyl cyclase from , is composed of a blue light using FAD (BLUF) domain fused to an adenylate cyclase (AC) domain. Since both the BLUF and AC domains are part of the same protein, OaPAC is a model for understanding how the ultrafast modulation of the chromophore binding pocket caused by photoexcitation results in the activation of the output domain on the μs-s time scale. In the present work, we use unnatural amino acid mutagenesis to identify specific sites in the protein that are involved in transducing the signal from the FAD binding site to the ATP binding site.

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