Abstract
The action of cytochrome P450 (P450) enzymes has been for years a very active arena of research that led to important insights, and generated lively debates over the nature of the various species and their reactivity patterns1. The active species of the enzyme is based on an iron ligated to a protoporphyrin IX macrocycle and two additional axial ligands (Figure 2.1): one, called proximal, is a thiolate from a cysteinate side chain of the protein and the other, called distal, is a variable ligand that changes during the cycle. When the distal ligand becomes an oxo group, the species is called Compound I (Cpd I), which is the reactive species of the enzyme and one of the most potent oxidants known in nature.
Original language | English |
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Title of host publication | Cytochrome P450 |
Subtitle of host publication | Structure, Mechanism, and Biochemistry: Third edition |
Publisher | Springer US |
Pages | 45-85 |
Number of pages | 41 |
ISBN (Print) | 9780306483240 |
DOIs | |
State | Published - 2005 |