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Micelle-modulated reactivity of novel copper(II) complexes with reduced L-histidine Schiff bases as mimic carboxylesterases.
- Source :
-
New Journal of Chemistry . 5/14/2024, Vol. 48 Issue 18, p8445-8453. 9p. - Publication Year :
- 2024
-
Abstract
- Two new copper(II) complexes (1 and 2) with reduced L -histidine Schiff bases were synthesized and characterized using single-crystal X-ray diffraction, powder X-ray diffraction, UV-visible spectroscopy, and thermal analysis. Single-crystal analysis reveals that 5-methyl-containing 1 possesses a simple phenoxo-bridged binuclear unit, while 5-bromine-substituted 2 possesses a metal–organic cage (MOC) structure. The as-prepared complexes as artificial metallohydrolases displayed catalytic activity towards the hydrolysis of both PNPP (p-nitrophenyl picolinate) and PNPA (p-nitrophenyl acetate). These two complexes provided 28-fold (for 1) and 39-fold (for 2) rate enhancements in comparison with spontaneous hydrolysis of PNPA, respectively. With regard to PNPP, its hydrolysis was accelerated by two orders of magnitude in the presence of 1 or 2. Additionally, positive micellar effects of bis(hexadecyldimethylammonium)hexane bromide (16-6-16) and N-octyldocosylammonium bromide (C22H45N(CH3)2C8H17Br, abbr. C22/8) were observed for the PNPA hydrolysis by 1 or 2, resulting in 1.3 to 3.9 times acceleration compared to that in buffered aqueous solution. In micellar solution of N,N-dimethyl-n-lauroylsarcosine sodium (LSS), no obvious rate enhancement was observed for the PNPA hydrolysis by 1 or 2. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 11440546
- Volume :
- 48
- Issue :
- 18
- Database :
- Academic Search Index
- Journal :
- New Journal of Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 177061843
- Full Text :
- https://doi.org/10.1039/d4nj00486h