Enzymatic Substrate Inhibition in Metal Free Catecholase Activity.
Kuntal PalSouvik BarmanJayanta BagPublished in: Chemistry & biodiversity (2023)
The catecholase activities were routinely modeled using transition metal complexes as catalyst and in some case basic pH were used as a reaction condition. In this article, the catalytic aerobic oxidation of proxy substrate 3,5-di-tert-butylcatechol (DTBC) in methanol using triethylamine/diethylamine as catalyst was demonstrated as a functional mimic of catecholase activity. The kinetic manifestation of DTBC oxidation was explained as enzymatic substrate inhibition pattern in Michaelis-Menten kinetic model. The mechanistic insight of the aerobic oxidation of DTBC was further validated using various spectroscopic techniques and DFT methods.
Keyphrases
- hydrogen peroxide
- visible light
- transition metal
- carbon dioxide
- molecular docking
- room temperature
- ionic liquid
- electron transfer
- highly efficient
- nitric oxide
- high intensity
- reduced graphene oxide
- structural basis
- metal organic framework
- amino acid
- escherichia coli
- pseudomonas aeruginosa
- cystic fibrosis
- staphylococcus aureus
- molecular dynamics