Symmetrical and unsymmetrical dizinc complexes as models for the active sites of hydrolytic enzymes.
Dinuclear carboxylate-bridged zinc complexes of one symmetric and one asymmetric phenolate-based ligand catalyse the transesterification of 2-hydroxypropyl-p-nitrophenyl phosphate (HPNP) at different rates, with an unsymmetrical complex being more active than a symmetric one.
Jarenmark
Martin
M
Inorganic Chemistry Research Group, Chemical Physics, Center for Chemistry and Chemical Engineering, Lund University, SE-221 00 Lund, Sweden.
Kappen
Sascha
S
Haukka
Matti
M
Nordlander
Ebbe
E
D002384:Catalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004950:Esterases / Q000737:chemistry; D006867:Hydrolases / Q000737:chemistry*; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D009942:Organometallic Compounds / Q000737:chemistry*; D010755:Organophosphates; D009943:Organophosphorus Compounds / Q000737:chemistry; D010636:Phenols / Q000737:chemistry; D011725:Pyridines / Q000737:chemistry; D015032:Zinc / Q000737:chemistry*
C436487:2-(hydroxypropyl)-4-nitrophenyl phosphate; D009942:Organometallic Compounds; D010755:Organophosphates; D009943:Organophosphorus Compounds; D010636:Phenols; D011725:Pyridines; D006867:Hydrolases; D004950:Esterases; D015032:Zinc