Catecholase Activity Study in Metal vs. Free Condition
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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).
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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).
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