Abstract
The complex multistep mechanism of oxygen activation in P450 is reviewed as a sequence of the following reactions: Substrate binding, reduction of the heme iron from ferric to the ferrous state, binding of dioxygen, second electron transfer and formation of peroxo-ferric intermediate, two sequential protonation events to give hydroperoxo-ferric intermediate, and finally, after O–O bond scission, the ferryl-oxo intermediate, termed compound I. Details of these processes and the role of interactions with redox partners, as well as substrate variability in the overall efficiency of P450 catalysis, are discussed. In addition, common points and variations between the soluble prokaryotic and membrane-bound eukaryotic cytochromes P450 with respect to the oxygen activation mechanisms are briefly compared.
| Original language | English (US) |
|---|---|
| Title of host publication | Cytochrome P450 |
| Subtitle of host publication | Structure, Mechanism, and Biochemistry, Fourth Edition |
| Publisher | Springer |
| Pages | 69-109 |
| Number of pages | 41 |
| ISBN (Electronic) | 9783319121086 |
| ISBN (Print) | 9783319121079 |
| DOIs | |
| State | Published - Jan 1 2015 |
Keywords
- Compound I
- Compound II
- Ferrous dioxygen complex (oxy-complex)
- Hydroperoxo intermediate
- Mössbauer spectroscopy
- Nanodiscs
- Oxygen binding
- O–O bond
- Peroxide dissociation
- Peroxo intermediate
- Raman (rR)
- Redox partner
- Redox potential
- Resonance
- Spin shift
- Substrate binding
- Superoxide
- Uncoupling
- Water ligand
ASJC Scopus subject areas
- General Pharmacology, Toxicology and Pharmaceutics
- General Biochemistry, Genetics and Molecular Biology
- General Medicine