Article

Interactions of cytochrome P450s with their ligands.

Department of Medicinal Chemistry, University of Washington, Seattle, WA 98195-7610, USA.
Archives of Biochemistry and Biophysics (impact factor: 2.93). 10/2010; 507(1):56-65. DOI:10.1016/j.abb.2010.10.006 pp.56-65
Source: PubMed

ABSTRACT Cytochrome P450s (CYPs) are heme-containing monooxygenases that contribute to an enormous range of enzymatic function including biosynthetic and detoxification roles. This review summarizes recent studies concerning interactions of CYPs with ligands including substrates, inhibitors, and diatomic heme-ligating molecules. These studies highlight the complexity in the relationship between the heme spin state and active site occupancy, the roles of water in directing protein-ligand and ligand-heme interactions, and the details of interactions between heme and gaseous diatomic CYP ligands. Both kinetic and thermodynamic aspects of ligand binding are considered.

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Keywords

active site occupancy
 
CYPs
 
Cytochrome P450s
 
detoxification roles
 
diatomic heme-ligating molecules
 
enormous range
 
gaseous diatomic CYP ligands
 
interactions
 
ligand binding
 
ligand-heme interactions
 
ligands
 
protein-ligand
 
review summarizes recent studies
 
substrates