Cytochrome P-450-CO and substrates: lessons from ligand binding under high pressure.
An overview of the application of high-pressure studies on the carbon monoxide complex of cytochrome P-450 is given. Different approaches to characterize ligand binding steps, the conformational states and substates and the compressibility of the ligand-bound complex are reviewed. A particular focus is the effect of substrates on these properties. It is shown that substrate mobility, compressibility and water accessibility are interrelated and may have functional meaning.
Jung
Christiane
C
Max-Delbrück-Center for Molecular Medicine, Protein Dynamics Laboratory, Berlin, Germany. cjung@mdc-berlin.de
D002248:Carbon Monoxide / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D006420:Hemeproteins / Q000737:chemistry; D006801:Humans; D006874:Hydrostatic Pressure; D008024:Ligands; D013379:Substrate Specificity
D006420:Hemeproteins; D008024:Ligands; D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System