The enzymatic substrate inhibition pattern was followed in the catalytic aerobic oxidation of 3,5-di-tert-butylcatechol (DTBC) in methanol utilising cyclic hindered base. The primary mechanistic finding for this aerobic oxidation was the reduction of one electron oxidation potential in the presence of base, which was confirmed by a variety of spectroscopic methods.

Abstract

Transition metal complexes as catalysts and, occasionally, basic pH as a reaction condition were employed to imitate the catecholase activity. Using morpholine/piperazine as a catalyst, under photo-mediated condition the catalytic aerobic oxidation of the proxy substrate 3,5-di-tert-butylcatechol (DTBC) in methanol very fast was shown in this article to be a functional mimic of catecholase activity. The Michaelis–Menten kinetic model's enzymatic substrate inhibition pattern was used to describe the kinetic manifestation of DTBC oxidation. Under photo-mediated condition the oxidation of DTBC was observed very fast which may be due to the higher energy increases the activation energy and under basic condition catechol oxidizes to o-quinone (DTBQ).