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8212386 
Journal Article 
Rapid, reversible oxygen atom transfer between an oxomanganese(V) porphyrin and bromide: A haloperoxidase mimic with enzymatic rates 
Woo, LK 
2003 
16 
1 
37-41 
English 
In studies of manganese metalloporphyrin complexes as models for cytochrome P-450 enzymes, formation of the high-valent oxo intermediate is the rate-determining step. Thus the oxometal species is short-lived and could not be characterized directly.13 The nature of this highly reactive transient had to be deduced from reactivity profiles and labeling experiments. The unusual stability of the oxometal complex, O = MnV(TM-2pyP), allows detailed mechanistic studies to be performed directly on the high-valent species. Extension of this approach to iron analogues should provide important chemical insights into heme-containing haloperoxidase processes as well as other heme-based monooxygenases.