Reconstitution of cytochrome P4502B4 (LM2) activity with camphor and linalool monooxygenase electron donors.
The P4502B4 (LM2) monooxygenase was shown to bind the P450cam and P450lin redoxins with respective dissociation constants of ca. 500 and 100 microM. When the redoxin reductases are added, the heterogeneous complexes demethylate benzphetamine with HCHO yields and Vmax similar to results with the homologous microsomal reductase. Implications of evolutionary conserved P450 redox electron donor binding site residues are discussed.
Bernhardt
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Max-Delbrueck-Center for Molecular Medicine, Berlin-Buch, Fr Germany.
Gunsalus
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IC
D000080462:Acyclic Monoterpenes; D001665:Binding Sites; D002164:Camphor / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D016650:Fluorescein-5-isothiocyanate / Q000378:metabolism; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D039821:Monoterpenes; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D013729:Terpenes / Q000378:metabolism*
D000080462:Acyclic Monoterpenes; D039821:Monoterpenes; D013729:Terpenes; D009243:NAD; D002164:Camphor; D003577:Cytochrome P-450 Enzyme System; C018584:linalool; D016650:Fluorescein-5-isothiocyanate