Asymmetric dinuclear metal complexes as models for active sites in hydrolases and redox enzymes

Research output: Contribution to journalReview articlepeer-review

Abstract

Recent advances in the synthesis of biomimetic asym. dinuclear transition metal complexes are reviewed. Emphasis is put on description of asym. model complexes for the active sites of the enzymes purple acid phosphatase, zinc phosphotriesterase, urease, Cu, Zn superoxide dismutase, tyrosinase, and catechol oxidase.
Original languageEnglish
Pages (from-to)433-462
JournalComptes Rendus. Chimie
Volume10
Issue number4-5
DOIs
Publication statusPublished - 2007

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

Free keywords

  • Enzyme functional sites Stereochemistry Transition metal complexes Enzymes
  • biological studies

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