Issue 3, 2014

Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes

Abstract

An enhanced understanding of the metal ion binding and active site structural features of phosphoesterases such as the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ), and the organophosphate degrading agent from Agrobacterium radiobacter (OpdA) have important consequences for potential applications. Coupled with investigations of the metalloenzymes, programs of study to synthesise and characterise model complexes based on these metalloenzymes can add to our understanding of structure and function of the enzymes themselves. This review summarises some of our work and illustrates the significance and contributions of model studies to knowledge in the area.

Graphical abstract: Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes

Article information

Article type
Perspective
Submitted
21 Aug 2013
Accepted
10 Oct 2013
First published
18 Oct 2013

Dalton Trans., 2014,43, 910-928

Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes

L. J. Daumann, G. Schenk, D. L. Ollis and L. R. Gahan, Dalton Trans., 2014, 43, 910 DOI: 10.1039/C3DT52287C

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