Enzymatic Substrate Inhibition in Metal Free Catecholase Activity

Abstract

AbstractThe 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.