Towards the Synthesis and Characterization of Functional Mimics: Xylose Glucose Isomerase, and Phosphoesterase in Aqueous Media

Date

2023

Authors

Gonzalez, Adrian

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Abstract

This work represents the research into the synthesis, characterization, and application of synthetic functional and/or structural mimics of the enzymes xylose/glucose isomerase (XGI) and phosphoester hydrolase. There is currently a lack of information in the literature regarding the mechanism behind both structural and functional biomimetic complexes of these enzymes. Two ligands were synthesized prior, H3camb and H5ccdp, and serve as the scaffolding to mimic the active site of phosphoesterase and XGI. New complexes of these ligands [Ga(camb)(H2O)2], [Ga(Hccdp)] and [Ga2(ccdp)(μ-OBz)(μ-SO4)] were synthesized and characterized using various spectroscopic techniques. Furthermore, these complexes were then used to investigate both sugar-binding and phosphoester hydrolysis using ESI-MS and various forms of spectroscopy. The kinetic studies showed the homodinuclear complex [Ga2(ccdp)(μ-OBz)(μ-SO4)]2- had a higher catalytic rate than the mononuclear complex [Ga(camb)(H2O)2]. ESI-MS also revealed the presence of multiple adducts with the substrates BNPP and PNPP. Additionally, based on the sugar-binding studies, it was found that both systems had a preference for binding to the anomeric C1 carbon of β-D-glucose. The homodinuclear complex [Ga2(ccdp)(μ-OBz)(μ-SO4)] exhibited a preference for coordinating with the C4 carbon instead of the C2 carbon in the second site. Additionally, neither variation displayed any inhibition in the presence of xylitol.

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Keywords

Structural mimics, Phosphoester hydrolase, Sugar-binding, Mononuclear complex, Kinetic studies

Citation

Department

Chemistry