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Structural and functional mimics of cytochromes P450

Woggon, Wolf-D.. (2007) Structural and functional mimics of cytochromes P450. Metal ions in life sciences, Vol. 3. pp. 27-55.

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Official URL: http://edoc.unibas.ch/dok/A5260219

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Abstract

A review on the competitive effort by inorg., org. and phys. chemists who synthesized/used enzyme models as a source to understand heme-thiolate monooxygenase catalysis.  In general, the natural structure has been simplified in various ways: the peripheric Me and vinyl substituents were omitted as well as in most cases the difficult-to-handle thiolate ligand.  For most of the complexes the meso-positions are substituted by Ph rings to prevent oxidn. at the meso-C atoms and further to provide a handle for functionalization.  In some cases the 3-pyrrole positions have been substituted with Me groups and Bu chains to render the complexes more sol. in org. solvents and to restrict conformational mobility of the Ph rings at the meso-positions.
Faculties and Departments:05 Faculty of Science
05 Faculty of Science > Departement Chemie > Chemie
UniBasel Contributors:Woggon, Wolf-Dietrich
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Note:Also published in: The ubiquitous roles of cytochrome P450 proteins. - Chichester : John Wiley, 2007. - S. 27-55 -- Publication type according to Uni Basel Research Database: Journal article
Last Modified:06 Nov 2015 10:21
Deposited On:22 Mar 2012 13:59

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