Symmetrical and unsymmetrical dizinc complexes as models for the active sites of hydrolytic enzymes.

Martin Jarenmark, Sascha Kappen, Matti Haukka, Ebbe Nordlander

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish
Pages (from-to)993-996
JournalDalton Transactions
Issue number8
DOIs
Publication statusPublished - 2008

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Chemical Physics (S) (011001060)

Subject classification (UKÄ)

  • Atom and Molecular Physics and Optics

Fingerprint

Dive into the research topics of 'Symmetrical and unsymmetrical dizinc complexes as models for the active sites of hydrolytic enzymes.'. Together they form a unique fingerprint.

Cite this