The importance of catalysts today as workhorses in most modern industrial fields cannot be downplayed. As a result, rational design and engineering of targeted catalysts have emerged as key objectives and are dependent on in-depth understanding of complex catalytic dynamics. Synchrotron radiation (SR) light sources with rich advanced experimental methods are being recognized as a comprehensive characterization platform, which can draw a full picture on such multiparameter-involved catalysis under actual working conditions. Herein, the recent progress of catalytic dynamics process studied by the means of various SR techniques is summarized. In particular, SR-based spectroscopic, scattering, and imaging investigations on true catalysts are first introduced with the potential of in situ and operando characterizations. Apparently, the limitations from single SR technique naturally prompt a simple combination of SR techniques to better understand the whole catalysis process. Moreover, the discrepancies among various online testing facilities and batches of samples, along with random/systematic errors introduced by traditional intermittent/asynchronous measurement make it imperative to develop more prolific systems, complementary of multiple SR techniques for deep probing of dynamic catalytic processes. It is believed that the booming new light sources can further enrich the current multiple SR techniques, and thus may realize the true visualization on future catalytic dynamic processes.

Download full-text PDF

Source
http://dx.doi.org/10.1002/adma.202205346DOI Listing

Publication Analysis

Top Keywords

catalytic dynamics
12
synchrotron radiation
8
light sources
8
multiple techniques
8
visualizing catalytic
4
dynamics processes
4
processes synchrotron
4
radiation multitechniques
4
multitechniques catalysts
4
catalysts today
4

Similar Publications

Identification of promising dipeptidyl peptidase-4 and protein tyrosine phosphatase 1B inhibitors from selected terpenoids through molecular modeling.

Bioinform Adv

December 2024

Structural and Computational Biology Group, Nutritional and Industrial Biochemistry Research Unit, Department of Biochemistry, College of Medicine, University of Ibadan, Ibadan 200005, Nigeria.

Motivation: Investigating novel drug-target interactions is crucial for expanding the chemical space of emerging therapeutic targets in human diseases. Herein, we explored the interactions of dipeptidyl peptidase-4 and protein tyrosine phosphatase 1B with selected terpenoids from African antidiabetic plants.

Results: Using molecular docking, molecular dynamics simulations, molecular mechanics with generalized Born and surface area solvation-free energy, and density functional theory analyses, the study revealed dipeptidyl peptidase-4 as a promising target.

View Article and Find Full Text PDF

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.

View Article and Find Full Text PDF

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.

View Article and Find Full Text PDF

Homology modeling and thermostability enhancement of PETase via hydrophobic interactions.

J Biomol Struct Dyn

January 2025

Enzyme and Microbial Technology Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.

The quest for sustainable solutions to plastic pollution has driven research into plastic-degrading enzymes, offering promising avenues for polymer recycling applications. However, enzymes derived from natural sources often exhibit suboptimal thermostability, hindering their industrial viability. Protein engineering techniques have emerged as a powerful approach to enhance the desired properties of these biocatalysts.

View Article and Find Full Text PDF

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.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!