Abstract
Abstract Two mono-Schiff base Mn(III) complexes (MnL2Cl, L=L1 and L2) were synthesized and employed as artificial hydrolases in catalyzing the hydrolysis of p-nitrophenylpicolinate (PNPP) in Gemini 16-2-16 micellar solution. The effect of different micelles and their complex structures on the catalytic hydrolysis of PNPP is discussed in detail. The observations showed that MnL 22Cl exhibited higher catalytic activity over MnL 12Cl under a comparable condition, which confirmed that an open active centre is essential for modulating the activities of the two enzyme mimics. Moreover, under the conditions employed, hydrolytic rates of PNPP induced by these Mn(III) complexes were faster in Gemini 16-2-16 micelles than that in the micellar solution of cetyltrimethylammonium bromide (CTAB), a conventional analogue of Gemini 16-2-16.
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