Interactions between redox partners in various cytochrome P450 systems: functional and structural aspects.
The various types of redox partner interactions employed in cytochrome P450 systems are described. The similarities and differences between the redox components in the major categories of P450 systems present in bacteria, mitochondria and microsomes are discussed in the light of the accumulated evidence from X-ray crystallographic and NMR spectroscopic determinations. Molecular modeling of the interactions between the redox components in various P450 mono-oxygenase systems is proposed on the basis of structural and mutagenesis information, together with experimental findings based on chemical modification of key residues likely to be associated with complementary binding sites on certain typical P450 isoforms and their respective redox partners.
Lewis
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DF
Molecular Toxicology Group, School of Biological Sciences, University of Surrey, Guildford, Surrey GU2 5XH, UK. d.lewis@surrey.ac.uk
Hlavica
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P
D000818:Animals; D001419:Bacteria / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism*; D004579:Electron Transport; D006418:Heme / Q000378:metabolism; D008861:Microsomes / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011199:Potentiometry; D013379:Substrate Specificity
D006418:Heme; D003577:Cytochrome P-450 Enzyme System