Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 4, Issue 21, Pages 3931-3937Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b611653a
Keywords
-
Categories
Funding
- Engineering and Physical Sciences Research Council [GR/S51059/01] Funding Source: researchfish
Ask authors/readers for more resources
The fundamental nature of reactivity in cytochrome P450 enzymes is currently controversial. Modelling of bacterial P450cam has suggested an important role for the haem propionates in the catalysis, though this finding has been questioned. Understanding the mechanisms of this enzyme family is important both in terms of basic biochemistry and potentially in the prediction of drug metabolism. We have modelled the hydroxylation of camphor by P450cam, using combined quantum mechanics/molecular mechanics (QM/MM) methods. A set of reaction pathways in the enzyme was determined. We were able to pinpoint the source of the discrepancies in the previous results. We show that when a correct ionization state is assigned to Asp297, no spin density appears on the haem propionates and the protein structure in this region remains preserved. These results indicate that the haem propionates are not involved in catalysis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available