Metalloporphyrines as Active Site AnaloguesLessons from Enzymes and Enzyme Models

Abstract

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 β-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.