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- W2025703072 abstract "In view of recent results from different sources, the reaction mechanisms of two heme-thiolate proteins, cytochrome P450cam and chloroperoxidase (CPO), are discussed. In this context a mechanism of CPO is proposed which includes H2O2 cleavage, subsequent formation of compound I and the identification of two elusive intermediates. The HOCl adduct of the iron(III)porpyhrin is the catalytically competent Cl+ donor chlorinating activated C-H bonds of substrates bound to the enzyme. Pulse-EPR characterization of an enzyme model of the resting state of P450cam suggests a role of the electric field of the protein for stabilizing the low-spin state of the cofactor of the enzyme. It is further suggested that the same effect of the protein may trigger the reactivity of compound I such that both concerted and two-step reactions are feasible within the concept of a Two-State-Reactivity. This review emphasizes the value of synthetic enzyme models complementing investigations of the native proteins." @default.
- W2025703072 created "2016-06-24" @default.
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- W2025703072 date "2001-02-01" @default.
- W2025703072 modified "2023-10-02" @default.
- W2025703072 title "Synthetic active site analogues of heme–thiolate proteins Characterization and identification of intermediates of the catalytic cycles of cytochrome P450cam and chloroperoxidase" @default.
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- W2025703072 doi "https://doi.org/10.1016/s0162-0134(00)00175-6" @default.
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