English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  DetailsSummary

Released
Journal Article

Reactions Catalyzed by Bacterial Cytochromes P450

MPS-Authors
/persons/resource/persons92561

Cryle,  Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Cytochrome P450, Max Planck Institute for Medical Research, Max Planck Society;
Heme and Flavin Enzymes, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://doi.org/10.1071/CH03040
(Any fulltext)

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Cryle, M., Stok, J. E., & De Voss, J. J. (2003). Reactions Catalyzed by Bacterial Cytochromes P450. Australien Journal of Chemistry, 56(8), 749-762. doi:10.1002/chin.200343234.


Cite as: https://hdl.handle.net/21.11116/0000-0000-3BE8-9
Abstract
The cytochromes P450 are a large family of oxidative haemoproteins that are responsible for a wide variety of oxidative transformations in a variety of organisms. This review focuses upon the reactions catalyzed specifically by bacterial enzymes, which includes aliphatic hydroxylation, alkene epoxidation, aromatic hydroxylation, oxidative phenolic coupling, heteroatom oxidation and dealkylation, and multiple oxidations including C−C bond cleavage. The potential for the practical application of the oxidizing power of these enzymes is briefly discussed