Data on electronic structures for the study of ligand effects on the zirconocene-mediated trimethylene carbonate polymerization

The data presented in this paper are related to the research article entitled “Effect of ligand structure in the trimethylene carbonate polymerization by cationic zirconocene catalysts: A “naked model” DFT study” (Jitonnom and Meelua, 2017) [1]. In this data article, we present 3D molecular information of 29 zirconocene catalysts that differ in electronic and steric properties. The data contains all cationic species along the initiation and first propagation step of the polymerization, which are provided in a PDB format that can be used for further studies

Computational evaluation of zirconocene catalysts for ε-caprolactone cationic ring-opening polymerization

Abstract This quantum chemical study presents the ligand effect and a structure–property relationship in the cationic ring-opening polymerization (CROP) of ε-caprolactone using zirconocene catalysts. We first examined the effects of catalyst structure on the initiation and chain propagation steps of the CROP process. A total of 54 catalyst structures were investigated to understand the influence of the ligand structure on the stability of the catalyst–monomer complex and polymerization activity. The properties of the catalysts were analyzed in terms of ancillary ligands, ligand substituents, and bridging units. Calculations showed that the polymerization follows a proposed cationic mechanism, with ring opening occurring via alkyl-bond cleavage. A correlation between complex stability and activation energy was also observed, with ligand substituents dominating in both steps. While the ancillary ligands directly affect the HOMO energy level, the bridges are mainly responsible for the catalyst geometries, resulting in reduced complex stability and higher activation energy for the propagation step. This study contributes to a better understanding of the structural characteristics of zirconocene catalysts, which offers guidance for improving CROP activities in lactone polymerization

A computational study of the reaction mechanism and stereospecificity of dihydropyrimidinase

Dihydropyrimidinase (DHPase) is a key enzyme in the pyrimidine pathway, the catabolic route for synthesis of β-amino acids. It catalyses the reversible conversion of 5,6-dihydrouracil (DHU) or 5,6-dihydrothymine (DHT) to the corresponding N-carbamoyl-β-amino acids. This enzyme has the potential to be used as a tool in the production of β-amino acids. Here, the reaction mechanism and origin of stereospecificity of DHPases from Saccharomyces kluyveri and Sinorhizobium meliloti CECT4114 were investigated and compared using a quantum mechanical cluster approach based on density functional theory. Two models of the enzyme active site were designed from the X-ray crystal structure of the native enzyme: a small cluster to characterize the mechanism and the stationary points and a large model to probe the stereospecificity and the role of stereo-gate-loop (SGL) residues. It is shown that a hydroxide ion first performs a nucleophilic attack on the substrate, followed by the abstraction of a proton by Asp358, which occurs concertedly with protonation of the ring nitrogen by the same residue. For the DHT substrate, the enzyme displays a preference for the l-configuration, in good agreement with experimental observation. Comparison of the reaction energetics of the two models reveals the importance of SGL residues in the stereospecificity of catalysis. The role of the conserved Tyr172 residue in transition-state stabilization is confirmed as the Tyr172Phe mutation increases the activation barrier of the reaction by ∼8 kcal mol−1. A detailed understanding of the catalytic mechanism of the enzyme could offer insight for engineering in order to enhance its activity and substrate scope