Metalloporphyrines as active site analogues--lessons from enzymes and enzyme models.
Research at the interface of enzyme chemistry and organic chemistry of metal complexes is particularly rewarding employing metal porphyrins as cofactor surrogates. Three examples are discussed: active site analogues of cytochrome P450 and chloroperoxidase (CPO), both heme-thiolate proteins, and enzyme models of beta-carotene monooxygenase, a non-heme iron protein. In all cases, catalytically active synthetic systems could be established displaying chemical reactivity close to the native proteins. Further, it is demonstrated that enzymatic reaction mechanisms can be elucidated by means of active site analogues (CPO) and information can be obtained from enzyme models that is useful to explain certain aspects of Nature's sophisticated approach to develop very efficient catalysts.
Woggon
Wolf-D
WD
Department of Chemistry, University of Basel, St. Johanns-Ring 19, CH-4056 Basel, Switzerland.
D001665:Binding Sites; D002711:Chloride Peroxidase / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D008958:Models, Molecular; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D010105:Oxygenases / Q000737:chemistry*; D011166:Porphyrins / Q000138:chemical synthesis / Q000737:chemistry*; D050559:beta-Carotene 15,15'-Monooxygenase
D009942:Organometallic Compounds; D011166:Porphyrins; D003577:Cytochrome P-450 Enzyme System; D002711:Chloride Peroxidase; D010105:Oxygenases; D050559:beta-Carotene 15,15'-Monooxygenase