This dataset contains research data for the publication "Mesoporous Confinement Enables Activity Boost in Cooperative Asymmetric Catalysis in Analogy to Enzymes".

Content: 1) Experimental Catalysis, Material Characterization, and Spectroscopy Data 2) Kinetics and Kinetic Modeling Data 3) Molecular Dynamics (MD) Simulations Data

1) Experimental Catalysis, Material Characterization, and Spectroscopy Data Data type and creation: The dataset comprises raw and processed experimental data focused on the synthesis and characterization of homogeneous and immobilized Cu(II) complexes, as well as the ordered mesoporous silica (OMS) support materials. It specifically includes data from: Electron Paramagnetic Resonance (EPR) spectroscopy Scanning Electron Microscopy (SEM) Transmission Electron Microscopy (TEM) Inductively Coupled Plasma Optical Emission Spectroscopy (ICP-OES) N2-physisorption (BET) Nuclear Magnetic Resonance (NMR) High-Resolution Mass Spectrometry (HRMS) Infrared (IR) and UV-Vis Spectroscopy Raw data from the catalytic 1,4-addition experiments Data structure: The dataset is organized into specific directories based on the applied analytical methods and materials. Data interpretation: The characterization data is used to confirm the successful synthesis and pore-selective immobilization of the catalysts. The morphological and spectroscopic measurements (SEM, TEM, EPR, ICP-OES) prove the structural integrity, uniform distribution, and restricted mobility of the catalysts within the mesoporous confinement. Reuse potential: The comprehensive characterization data serves as a reference for researchers working on catalysis and mesoporous materials. Furthermore, the detailed raw data allows other researchers to precisely reproduce the complex catalyst syntheses, immobilization protocols, and catalytic evaluations.

2) Kinetics and Kinetic Modeling Data Data type and creation: This section contains concentration-time course data obtained via GC-MS measurements at various temperatures, as well as the data and scripts utilized for the Eyring kinetics modeling. Data structure: The dataset is separated into experimental kinetics data and computational modeling files. Data interpretation: Five concentration-time courses per reaction system were jointly fitted to extract system-specific activation parameters (enthalpy, entropy, and Gibbs free energy of activation). Reuse potential: The kinetic data and modeling approach can be reused by physical and computational chemists to benchmark new kinetic models or to compare confinement effects across different catalytic systems.

3) Molecular Dynamics (MD) Simulations Data Data type and creation: This part includes files associated with the performed MD simulations. Data structure: Organized by simulation environment (bulk vs. specific pore sizes) and surface chemistry. Data interpretation: The MD simulations are utilized to calculate radial density profiles and Cu-H distance distributions. Reuse potential: The trajectories and topologies provide a valuable starting point for theoretical chemists aiming to study confined solvent effects or to simulate structurally modified catalyst derivatives under similar mesoporous conditions.

Abstract: Enzymes achieve substantial rate accelerations by combining cooperative functional group activation with confinement inside organized active sites, which reduce entropic costs and enforce productive orientations of activated substrates. Here, we translate these principles into artificial cooperative asymmetric catalysis using mesoporous confinement. Embedding a chiral bifunctional catalyst into ordered mesoporous silica creates a synthetic analogue of enzymatic pockets, in which cooperative activation and nanoscale confinement act synergistically. By such confinement, reaction half-lives could be reduced by up to 97% in asymmetric 1,4-additions. Kinetic analyses attribute this enhancement to entropic advantages of confinement, while molecular dynamics simulations reveal narrowing of the catalyst’s conformational space closely paralleling the enzymatic preorganization as molecular origin. Unlike enzymes, however, the mesoporous framework remains tunable, allowing linker length and pore size to systematically adjust reactivity. This work establishes confinement engineering as a modular strategy to design “unnatural active sites” that merge enzymatic efficiency with synthetic catalyst flexibility. It could thus bridge the gap between nature’s precision and the versatility of synthetic chemistry.