Structural and functional mimics of cytochromes P450

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.